Solution NMR views of dynamical ordering of biomacromolecules
To understand the mechanisms related to the ‘dynamical ordering’ of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can inves...
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| Published in | Biochimica et biophysica acta Vol. 1862; no. 2; pp. 287 - 306 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier B.V
01.02.2018
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| Abstract | To understand the mechanisms related to the ‘dynamical ordering’ of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can investigate biophysical events at the atomic level, in near-physiological buffer solutions, or even inside cells.
In the past several decades, progress in solution NMR has significantly contributed to the elucidation of three-dimensional structures, the understanding of conformational motions, and the underlying thermodynamic and kinetic properties of biomacromolecules. This review discusses recent methodological development of NMR, their applications and some of the remaining challenges.
Although a major drawback of NMR is its difficulty in studying the dynamical ordering of larger biomolecular systems, current technologies have achieved considerable success in the structural analysis of substantially large proteins and biomolecular complexes over 1MDa and have characterised a wide range of timescales across which biomolecular motion exists. While NMR is well suited to obtain local structure information in detail, it contributes valuable and unique information within hybrid approaches that combine complementary methodologies, including solution scattering and microscopic techniques.
For living systems, the dynamic assembly and disassembly of macromolecular complexes is of utmost importance for cellular homeostasis and, if dysregulated, implied in human disease. It is thus instructive for the advancement of the study of the dynamical ordering to discuss the potential possibilities of solution NMR spectroscopy and its applications. This article is part of a Special Issue entitled “Biophysical Exploration of Dynamical Ordering of Biomolecular Systems” edited by Dr. Koichi Kato.
•Solution NMR is an ideal tool to study dynamical ordering of biomacromolecules.•Biomolecular dynamics over a broad range of timescales can be characterised by NMR.•Current NMR techniques can deal with huge supramolecular machinery over 1MDa.•NMR approach also enables studying protein structures and dynamics in living cells. |
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| AbstractList | To understand the mechanisms related to the 'dynamical ordering' of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can investigate biophysical events at the atomic level, in near-physiological buffer solutions, or even inside cells.BACKGROUNDTo understand the mechanisms related to the 'dynamical ordering' of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can investigate biophysical events at the atomic level, in near-physiological buffer solutions, or even inside cells.In the past several decades, progress in solution NMR has significantly contributed to the elucidation of three-dimensional structures, the understanding of conformational motions, and the underlying thermodynamic and kinetic properties of biomacromolecules. This review discusses recent methodological development of NMR, their applications and some of the remaining challenges.SCOPE OF REVIEWIn the past several decades, progress in solution NMR has significantly contributed to the elucidation of three-dimensional structures, the understanding of conformational motions, and the underlying thermodynamic and kinetic properties of biomacromolecules. This review discusses recent methodological development of NMR, their applications and some of the remaining challenges.Although a major drawback of NMR is its difficulty in studying the dynamical ordering of larger biomolecular systems, current technologies have achieved considerable success in the structural analysis of substantially large proteins and biomolecular complexes over 1MDa and have characterised a wide range of timescales across which biomolecular motion exists. While NMR is well suited to obtain local structure information in detail, it contributes valuable and unique information within hybrid approaches that combine complementary methodologies, including solution scattering and microscopic techniques.MAJOR CONCLUSIONSAlthough a major drawback of NMR is its difficulty in studying the dynamical ordering of larger biomolecular systems, current technologies have achieved considerable success in the structural analysis of substantially large proteins and biomolecular complexes over 1MDa and have characterised a wide range of timescales across which biomolecular motion exists. While NMR is well suited to obtain local structure information in detail, it contributes valuable and unique information within hybrid approaches that combine complementary methodologies, including solution scattering and microscopic techniques.For living systems, the dynamic assembly and disassembly of macromolecular complexes is of utmost importance for cellular homeostasis and, if dysregulated, implied in human disease. It is thus instructive for the advancement of the study of the dynamical ordering to discuss the potential possibilities of solution NMR spectroscopy and its applications. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato.GENERAL SIGNIFICANCEFor living systems, the dynamic assembly and disassembly of macromolecular complexes is of utmost importance for cellular homeostasis and, if dysregulated, implied in human disease. It is thus instructive for the advancement of the study of the dynamical ordering to discuss the potential possibilities of solution NMR spectroscopy and its applications. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato. To understand the mechanisms related to the ‘dynamical ordering’ of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can investigate biophysical events at the atomic level, in near-physiological buffer solutions, or even inside cells.In the past several decades, progress in solution NMR has significantly contributed to the elucidation of three-dimensional structures, the understanding of conformational motions, and the underlying thermodynamic and kinetic properties of biomacromolecules. This review discusses recent methodological development of NMR, their applications and some of the remaining challenges.Although a major drawback of NMR is its difficulty in studying the dynamical ordering of larger biomolecular systems, current technologies have achieved considerable success in the structural analysis of substantially large proteins and biomolecular complexes over 1MDa and have characterised a wide range of timescales across which biomolecular motion exists. While NMR is well suited to obtain local structure information in detail, it contributes valuable and unique information within hybrid approaches that combine complementary methodologies, including solution scattering and microscopic techniques.For living systems, the dynamic assembly and disassembly of macromolecular complexes is of utmost importance for cellular homeostasis and, if dysregulated, implied in human disease. It is thus instructive for the advancement of the study of the dynamical ordering to discuss the potential possibilities of solution NMR spectroscopy and its applications. This article is part of a Special Issue entitled “Biophysical Exploration of Dynamical Ordering of Biomolecular Systems” edited by Dr. Koichi Kato. To understand the mechanisms related to the 'dynamical ordering' of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can investigate biophysical events at the atomic level, in near-physiological buffer solutions, or even inside cells. In the past several decades, progress in solution NMR has significantly contributed to the elucidation of three-dimensional structures, the understanding of conformational motions, and the underlying thermodynamic and kinetic properties of biomacromolecules. This review discusses recent methodological development of NMR, their applications and some of the remaining challenges. Although a major drawback of NMR is its difficulty in studying the dynamical ordering of larger biomolecular systems, current technologies have achieved considerable success in the structural analysis of substantially large proteins and biomolecular complexes over 1MDa and have characterised a wide range of timescales across which biomolecular motion exists. While NMR is well suited to obtain local structure information in detail, it contributes valuable and unique information within hybrid approaches that combine complementary methodologies, including solution scattering and microscopic techniques. For living systems, the dynamic assembly and disassembly of macromolecular complexes is of utmost importance for cellular homeostasis and, if dysregulated, implied in human disease. It is thus instructive for the advancement of the study of the dynamical ordering to discuss the potential possibilities of solution NMR spectroscopy and its applications. This article is part of a Special Issue entitled "Biophysical Exploration of Dynamical Ordering of Biomolecular Systems" edited by Dr. Koichi Kato. To understand the mechanisms related to the ‘dynamical ordering’ of macromolecules and biological systems, it is crucial to monitor, in detail, molecular interactions and their dynamics across multiple timescales. Solution nuclear magnetic resonance (NMR) spectroscopy is an ideal tool that can investigate biophysical events at the atomic level, in near-physiological buffer solutions, or even inside cells. In the past several decades, progress in solution NMR has significantly contributed to the elucidation of three-dimensional structures, the understanding of conformational motions, and the underlying thermodynamic and kinetic properties of biomacromolecules. This review discusses recent methodological development of NMR, their applications and some of the remaining challenges. Although a major drawback of NMR is its difficulty in studying the dynamical ordering of larger biomolecular systems, current technologies have achieved considerable success in the structural analysis of substantially large proteins and biomolecular complexes over 1MDa and have characterised a wide range of timescales across which biomolecular motion exists. While NMR is well suited to obtain local structure information in detail, it contributes valuable and unique information within hybrid approaches that combine complementary methodologies, including solution scattering and microscopic techniques. For living systems, the dynamic assembly and disassembly of macromolecular complexes is of utmost importance for cellular homeostasis and, if dysregulated, implied in human disease. It is thus instructive for the advancement of the study of the dynamical ordering to discuss the potential possibilities of solution NMR spectroscopy and its applications. This article is part of a Special Issue entitled “Biophysical Exploration of Dynamical Ordering of Biomolecular Systems” edited by Dr. Koichi Kato. •Solution NMR is an ideal tool to study dynamical ordering of biomacromolecules.•Biomolecular dynamics over a broad range of timescales can be characterised by NMR.•Current NMR techniques can deal with huge supramolecular machinery over 1MDa.•NMR approach also enables studying protein structures and dynamics in living cells. |
| Author | Lee, Donghan Ito, Yutaka Griesinger, Christian Ikeya, Teppei Ban, David Kato, Koichi |
| Author_xml | – sequence: 1 givenname: Teppei surname: Ikeya fullname: Ikeya, Teppei email: tikeya@tmu.ac.jp organization: Department of Chemistry, Graduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, Tokyo 192-0373, Japan – sequence: 2 givenname: David surname: Ban fullname: Ban, David organization: Department of Medicine, James Graham Brown Cancer Center, University of Louisville, 505 S. Hancock St., Louisville, KY 40202, USA – sequence: 3 givenname: Donghan surname: Lee fullname: Lee, Donghan organization: Department of Medicine, James Graham Brown Cancer Center, University of Louisville, 505 S. Hancock St., Louisville, KY 40202, USA – sequence: 4 givenname: Yutaka surname: Ito fullname: Ito, Yutaka organization: Department of Chemistry, Graduate School of Science and Engineering, Tokyo Metropolitan University, 1-1 Minamiosawa, Hachioji, Tokyo 192-0373, Japan – sequence: 5 givenname: Koichi surname: Kato fullname: Kato, Koichi organization: Okazaki Institute for Integrative Bioscience and Institute for Molecular Science, National Institutes of Natural Sciences, 5-1 Higashiyama, Myodaiji, Okazaki 444-8787, Japan – sequence: 6 givenname: Christian surname: Griesinger fullname: Griesinger, Christian email: cigr@nm.mpibpc.mpg.de organization: Department of Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen 37077, Germany |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28847507$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1021/ja062146p 10.1016/j.jmr.2009.10.008 10.1073/pnas.1103270108 10.1063/1.1755656 10.1002/cbic.200600551 10.1016/j.jmr.2010.09.014 10.1126/science.1067680 10.1016/j.jmr.2006.06.007 10.1002/anie.201207266 10.1007/s10858-016-0020-6 10.1073/pnas.0408930102 10.1021/ja00381a010 10.1016/j.jmr.2016.05.013 10.1007/s10858-013-9769-z 10.1007/s10858-011-9502-8 10.1021/bi00020a025 10.1073/pnas.0700930104 10.1038/nrd1129 10.1023/A:1008319130714 10.1002/anie.201105086 10.1002/cbic.201402677 10.1038/nature02655 10.1016/j.jmr.2007.07.008 10.1038/nmeth.3695 10.1038/nmat2764 10.1021/ja048738u 10.1023/A:1023076212536 10.1021/ja102296k 10.1073/pnas.0800256105 10.1021/acs.biochem.5b00820 10.1016/S0079-6565(00)00028-5 10.1007/s10858-006-0001-2 10.1016/j.sbi.2003.09.009 10.1021/ja072717t 10.1007/s10858-012-9626-5 10.1016/j.bbrc.2013.07.127 10.1021/cr400695p 10.1021/ja202259a 10.1007/s10858-006-9079-9 10.1007/s10858-016-0059-4 10.1126/science.1749933 10.1007/BF00219946 10.1126/science.1233066 10.1021/ja000976b 10.1038/msb.2011.82 10.1021/bi00138a003 10.1021/ja9835887 10.1023/B:JNMR.0000013706.09264.36 10.1039/C6CC05490K 10.1021/bi900712r 10.1021/ja051306e 10.1021/ja984390p 10.1007/128_2011_215 10.1021/ja0367041 10.1007/s10858-011-9541-1 10.1073/pnas.94.23.12366 10.1007/s10858-005-0658-y 10.1016/j.jmr.2012.05.005 10.1002/anie.201100370 10.1016/j.ymeth.2004.03.014 10.1371/journal.pone.0043725 10.1016/j.pnmrs.2010.03.001 10.1016/j.pnmrs.2011.05.001 10.1016/j.bpj.2015.06.069 10.1002/pro.153 10.1016/j.pnmrs.2010.04.003 10.1021/ja0687668 10.1023/A:1008399320576 10.1021/ja310928u 10.1021/mp200615m 10.1016/j.str.2013.04.001 10.1021/ja030153x 10.1016/j.sbi.2013.01.007 10.1073/pnas.0907195106 10.1023/A:1024710729352 10.1146/annurev.biophys.37.032807.125817 10.1038/nature18965 10.1038/nature07814 10.1126/science.1079731 10.1016/j.chembiol.2014.09.001 10.1021/bi100727y 10.1126/science.1191723 10.1021/cr0404287 10.1021/ja9933184 10.1021/bi961896g 10.1073/pnas.1218414109 10.1006/jmre.2001.2466 10.1021/ja00151a018 10.1006/jmbi.1996.0603 10.1073/pnas.1322079111 10.1038/nature07839 10.1016/j.str.2009.08.001 10.1126/science.1250494 10.1073/pnas.1511308112 10.1021/bi201496d 10.1021/ja9052027 10.1021/ja00168a070 10.1016/j.jmb.2008.11.055 10.1021/jp2081116 10.1021/ja403091c 10.1038/nmeth900 10.1038/nbt1519 10.1021/ja206442c 10.1021/ja809526q 10.7554/eLife.13571 10.1006/jmre.1999.1980 10.1093/protein/12.9.713 10.1002/cbic.200500124 10.1088/1742-6596/699/1/012005 10.1021/ja407509z 10.1021/ar700132n 10.1073/pnas.1510083112 10.1021/ja993845n 10.1021/acs.jpclett.6b01074 10.1021/ja8086278 10.1007/s00249-008-0367-z 10.1038/srep38312 10.1021/acs.chemrev.6b00177 10.1007/s10858-015-9923-x 10.1021/cr030413t 10.1021/ja980832l 10.1021/ja907476w 10.1021/ja908004w 10.1021/ja0204776 10.1021/ja026939x 10.1021/ja983434r 10.1002/cbic.201200737 10.1039/C5CP06197K 10.1007/s10858-013-9775-1 10.1021/ja00074a073 10.1021/ja031580d 10.1146/annurev.biophys.30.1.129 10.1126/science.278.5340.1111 10.1021/ja304809s 10.1007/s10858-008-9280-0 10.1038/nature05959 10.1038/nature09444 10.1006/jmbi.1996.0581 10.1021/ar700189y 10.1038/nchembio.596 10.1021/ja3001419 10.1038/nchembio.232 10.1002/prot.21723 10.1038/nature16531 10.1038/nsb0497-292 10.1021/ja211115q 10.1126/science.276.5316.1230 10.1021/jacs.6b02424 10.1002/anie.201305094 10.1038/nature04525 10.1021/ja803213p 10.1016/S0006-3495(02)75241-7 10.1073/pnas.1611418113 10.1007/s00249-011-0754-8 10.1186/1472-6807-7-31 10.1002/cbic.201000610 10.1002/pro.2797 10.1023/A:1008383205836 10.1017/S0033583514000122 10.1073/pnas.0407792102 10.1006/jmbi.2001.5235 10.1002/anie.201406145 10.1007/s10858-008-9294-7 10.1073/pnas.1518620113 10.1021/ja202397p 10.1002/anie.201405180 10.3390/molecules181011904 10.1093/nar/gki615 10.1038/nprot.2010.69 10.1016/j.jmr.2005.08.014 10.1006/jmbi.1997.1588 10.1002/pro.2643 10.1007/s12551-015-0166-6 10.1038/nature09775 10.1038/nchembio.1250 10.1126/science.1184991 10.1073/pnas.1213640109 10.1073/pnas.0507603102 10.1038/nchembio.1202 10.1038/nmeth.1280 10.1023/A:1018631009583 10.1021/ja068541x 10.1021/ja807893k 10.1016/j.cell.2013.03.034 10.1002/anie.201408890 10.1073/pnas.0708296104 10.1002/pro.2538 10.1111/j.1432-1033.1979.tb13137.x 10.1021/ja9708676 10.1023/A:1008339928400 10.1007/s10858-015-9954-3 10.1021/ja200461n 10.1073/pnas.0505129102 10.1007/s10858-016-0072-7 10.1038/nature10577 10.1021/ar400244v 10.1021/cr900033p 10.1021/ja300265w 10.1007/s10858-006-9127-5 10.1021/bi061943x 10.1038/nature05512 10.1073/pnas.1305688110 10.1007/s10858-013-9705-2 10.1021/ja305091n 10.1126/science.7754375 10.1016/j.cell.2007.09.039 10.1021/ja0564158 10.1021/ja0057528 10.1038/nature13001 10.1016/S0968-0004(01)01938-7 10.1063/1.1734121 10.1073/pnas.051429498 10.1021/acs.chemrev.5b00548 10.1038/nature11271 10.1073/pnas.1515366112 10.1021/jacs.6b01447 10.1038/nature06389 10.1021/bi00449a003 10.1002/anie.201100440 10.1021/cr040429z 10.1021/ja982592f 10.1021/ja054342m 10.1021/ja00097a084 10.1038/nsb1095-865 10.1006/jmbi.1997.1284 10.1021/ja904407w 10.1016/j.jmb.2014.07.019 10.1002/anie.201207243 10.1073/pnas.1519609113 10.1006/jmbi.2000.3842 10.1021/ja2010048 10.1021/ja001432c 10.1007/s10858-008-9244-4 10.1007/s10858-016-0081-6 10.1007/s10858-013-9811-1 10.1126/science.1157092 10.1016/S0076-6879(94)39004-5 10.1021/ja104578n 10.1016/S0079-6565(01)00043-7 10.1021/ja0761784 10.1021/ja054842f 10.1021/ja0761636 10.1016/j.jmr.2008.02.003 10.1002/ange.201603501 10.1007/s10858-007-9211-5 10.1021/ja808616v 10.1073/pnas.0604667103 10.1021/ja9706514 10.1007/s00249-005-0037-3 10.1038/nsb0697-443 10.1038/nsb1101-926 10.1002/anie.201500261 10.1021/ja400920w 10.1021/ja010002z 10.1007/s10858-016-0055-8 10.1007/s10858-012-9611-z 10.1021/ja067827z 10.1073/pnas.121069998 10.1021/acs.jpcb.6b02024 10.1006/jmbi.1997.1553 10.1021/ja0261123 10.1002/anie.200801492 |
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| References | Theillet, Binolfi, Bekei, Martorana, Rose, Stuiver, Verzini, Lorenz, van Rossum, Goldfarb, Selenko (bb1190) 2016; 530 Fischer, Kloiber, Häusler, Ledolter, Konrat, Schmid (bb0840) 2007; 8 Ma, Kumar, Tsai, Nussinov (bb0465) 1999; 12 Korzhnev, Salvatella, Vendruscolo, Di Nardo, Davidson, Dobson, Kay (bb0685) 2004; 430 Tugarinov, Kay (bb1070) 2004; 126 Pervushin, Riek, Wider, Wüthrich (bb0220) 1997; 94 Markwick, Bouvignies, Salmon, McCammon, Nilges, Blackledge (bb0485) 2009; 131 Balbach, Forge, van Nuland, Winder, Hore, Dobson (bb0755) 1995; 2 Beck (bb1370) 1979; 97 Luginbuhl, Wutrich (bb0130) 2002; 40 Ban, Funk, Gulich, Egger, Sabo, Walter, Fenwick, Giller, Pichierri, de Groot, Lange, Grubmüller, Salvatella, Wolf, Loidl, Kree, Becker, Lakomek, Lee, Lunkenheimer, Griesinger (bb0630) 2011; 50 Pervushin, Riek, Wider, Wuthrich (bb0880) 1997; 94 Key, Bhattacharyya, Morcrette, Seznec, Tarascon, Grey (bb0775) 2009; 131 Gardner, Kay (bb0815) 1997; 119 Tugarinov, Choy, Orekhov, Kay (bb0400) 2005; 102 Pervushin, Braun, Fernandez, Wuthrich (bb0885) 2000; 17 Ellis (bb1260) 2001; 26 Korzhnev, Skrynnikov, Millet, Torchia, Kay (bb0195) 2002; 124 Ferrage, Reichel, Battacharya, Cowburn, Ghose (bb0205) 2010; 207 Linnet, Teilum (bb0965) 2016; 64 Stern, Donoho, Hoch (bb0980) 2007; 188 Abyzov, Salvi, Schneider, Maurin, Ruigrok, Jensen, Blackledge (bb0270) 2016; 138 Grishaev, Wu, Trewhella, Bax (bb1045) 2005; 127 Csizmok, Follis, Kriwacki, Forman-Kay (bb0120) 2016; 116 Lakomek, Walter, Farès, Lange, de Groot, Grubmüller, Brüschweiler, Munk, Becker, Meiler, Griesinger (bb0250) 2008; 41 Xue, Podkorytov, Rao, Benjamin, Sun, Skrynnikov (bb0285) 2009; 18 Cervantes, Markwick, Sue, McCammon, Dyson, Komives (bb0500) 2009; 48 Brüschweiler, Liao, Wright (bb0245) 1995; 268 Yang, Takeda, Terauchi, Jee, Kainosho (bb0870) 2015; 54 Palmer (bb0210) 2004; 104 Korzhnev, Kay (bb0610) 2008; 41 Isaacson, Simpson, Liu, Cota, Zhang, Freemont, Matthews (bb0835) 2007; 129 Trott, Palmer (bb0620) 2002; 154 Ikeya, Jee, Shigemitsu, Hamatsu, Mishima, Ito, Kainosho, Guntert (bb1325) 2011; 50 Selenko, Serber, Gade, Ruderman, Wagner (bb1175) 2006; 103 Robustelli, Stafford, Palmer (bb0380) 2012; 134 Keskin (bb0070) 2007; 7 Latham, Sekhar, Kay (bb1160) 2014; 111 Nicholson, Kay, Baldisseri, Arango, Young, Bax, Torchia (bb0295) 1992; 31 Opitz, Isogai, Grzesiek (bb0795) 2015; 62 Latham, Kay (bb1310) 2014; 426 Bax, Vuister, Grzesiek, Delaglio, Wang, Tschudin, Zhu (bb0395) 1994; 239 Kubo, Nishida, Udagawa, Takarada, Ogino, Shimada (bb1345) 2013; 52 Ozbabacan, Gursoy, Keskin, Nussinov (bb0095) 2010; 13 Loria, Berlow, Watt (bb0045) 2008; 41 Mobli, Stern, Hoch (bb0900) 2006; 182 Nobeli, Favia, Thornton (bb0025) 2009; 27 Korzhnev (bb0185) 1997; 127 Jensen, Communie, Ribeiro, Martinez, Desfosses, Salmon, Mollica, Gabel, Jamin, Longhi, Ruigrok, Blackledge (bb0355) 2011; 108 Barnes, Monteith, Pielak (bb1295) 2011; 12 Jaravine, Orekhov (bb0940) 2006; 128 Holland, Bostock, Gladden, Nietlispach (bb0975) 2011; 50 Korzhnev, Billeter, Arseniev, Orekhov (bb0145) 2001; 38 Ban, Mazur, Carneiro, Sabo, Giller, Koharudin, Becker, Gronenborn, Griesinger, Lee (bb0735) 2013; 57 Matsuki, Konuma, Fujiwara, Sugase (bb0960) 2011; 115 Salmon, Bascom, Andricioaei, Al-Hashimi (bb0455) 2013; 135 Smith, Ban, Pratihar, Giller, Schwiegk, de Groot, Becker, Griesinger, Lee (bb0605) 2015; 54 Meiler, Prompers, Peti, Griesinger, Brüschweiler (bb0410) 2001; 123 Latorraca, Venkatakrishnan, Dror (bb0110) 2017; 117 Dominguez, Boelens, Bonvin (bb1090) 2003; 125 Schroghuber, Sara, Bisaccia, Schmid, Konrat, Lichtenecker (bb0855) 2015; 16 Inomata, Ohno, Tochio, Isogai, Tenno, Nakase, Takeuchi, Futaki, Ito, Hiroaki, Shirakawa (bb1195) 2009; 458 Schwalbe, Fiebig, Buck, Jones, Grimshaw, Spencer, Glaser, Smith, Dobson (bb0275) 1997 Stelzer, Frank, Kratz, Swanson, Gonzalez-Hernandez, Lee, Andricioaei, Markovitz, Al-Hashimi (bb0475) 2011; 7 Shen, Lange, Delaglio, Rossi, Aramini, Liu, Eletsky, Wu, Singarapu, Lemak, Ignatchenko, Arrowsmith, Szyperski, Montelione, Baker, Bax (bb1360) 2008; 105 Mayzel, Rosenlow, Isaksson, Orekhov (bb0950) 2014; 58 Bertrand, Reverdatto, Burz, Zitomer, Shekhtman (bb1170) 2012; 134 Lee, Hilty, Wider, Wüthrich (bb0225) 2006; 178 Sinha, Jen-Jacobson, Rule (bb0820) 2011; 50 Glaeser (bb0010) 2016; 13 Miklos, Li, Sharaf, Pielak (bb1265) 2010; 49 Motlagh, Wrabl, Li, Hilser (bb0050) 2014; 508 Kroenke, Loria, Lee, Rance, Palmer (bb0215) 1998; 120 Brüschweiler, Wright (bb0425) 1994; 116 Gabel, Simon, Sattler (bb1050) 2006; 35 Kainosho, Torizawa, Iwashita, Terauchi, Mei Ono, Guntert (bb0865) 2006; 440 Libich, Tugarinov, Clore (bb0720) 2015; 112 Korzhnev, Religa, Banachewicz, Fersht, Kay (bb0650) 2010; 329 Tzeng, Kalodimos (bb0085) 2013; 9 Berjanskii, Wishart (bb0370) 2013; 135 Zhou, Rivas, Minton (bb1275) 2008; 37 Hikone, Hirai, Mishima, Inomata, Ikeya, Arai, Shirakawa, Sodeoka, Ito (bb1355) 2016; 66 Tugarinov, Choy, Orekhov, Kay (bb1065) 2005; 102 Ayala, Sounier, Use, Gans, Boisbouvier (bb0825) 2009; 43 Brocchieri, Karlin (bb1080) 2005; 33 Arkin, Tang, Wells (bb0035) 2014; 21 Tugarinov, Sprangers, Kay (bb1130) 2007; 129 Tjandra, Garrett, Gronenborn, Bax, Clore (bb0160) 1997; 4 Chen, Tjandra (bb1030) 2012; 326 Haupt, Patzschke, Weininger, Gröger, Kovermann, Balbach (bb0740) 2011; 133 Beck, Schmidt, Malmstroem, Claassen, Ori, Szymborska, Herzog, Rinner, Ellenberg, Aebersold (bb1375) 2011; 7 Hansen, Yang, Feng, Zhou, Wiesner, Bai, Kay (bb0170) 2007; 129 Ban, Sabo, Griesinger, Lee (bb0165) 2013; 18 Tzeng, Kalodimos (bb0325) 2012; 488 Barna, Laue, Mayger, Skilling, Worrall (bb0905) 1987; 73 Kazimierczuk, Zawadzka, Kozminski (bb0915) 2008; 192 Chiarparin, Pelupessy, Ghose, Bodenhausen (bb0530) 2000; 122 Khan, Charlier, Augustyniak, Salvi, Dejean, Bodenhausen, Lequin, Pelupessy, Ferrage (bb0260) 2015; 109 Theillet, Binolfi, Frembgen-Kesner, Hingorani, Sarkar, Kyne, Li, Crowley, Gierasch, Pielak, Elcock, Gershenson, Selenko (bb0255) 2014; 114 Gasper, Fuglestad, Komives, Markwick, McCammon (bb0495) 2012; 109 Guntert, Mumenthaler, Wuthrich (bb1105) 1997; 273 Guijarro, Morton, Plaxco, Campbell, Dobson (bb0765) 1998; 276 Hansel, Foldynova-Trantirkova, Lohr, Buck, Bongartz, Bamberg, Schwalbe, Dotsch, Trantirek (bb1230) 2009; 131 Pratihar, Sabo, Ban, Fenwick, Becker, Salvatella, Griesinger, Lee (bb0440) 2016; 128 Bowen, Hilty (bb0785) 2008; 47 Baldwin, Religa, Hansen, Bouvignies, Kay (bb0660) 2010; 132 Frederick, Marlow, Valentine, Wand (bb0315) 2007; 448 Iwahara, Schwieters, Clore (bb1005) 2004; 126 Matsuki, Eddy, Herzfeld (bb0955) 2009; 131 Berjanskii, Wishart (bb0375) 2005; 127 Hamatsu, O'Donovan, Tanaka, Shirai, Hourai, Mikawa, Ikeya, Mishima, Boucher, Smith, Laue, Shirakawa, Ito (bb0935) 2013; 135 Liu, Xu, Cowburn (bb1210) 2009; 462 Farber, Mittermaier (bb0670) 2015; 7 Grishaev, Tugarinov, Kay, Trewhella, Bax (bb1055) 2008; 40 Ikeya, Hanashima, Hosoya, Shimazaki, Ikeda, Mishima, Güntert, Ito (bb1340) 2016; 6 Akke, Brüschweiler, Palmer (bb0320) 1993; 115 Carlomagno, Maurer, Hennig, Griesinger (bb0525) 2000; 122 Xue, Kellogg, Kimsey, Sathyamoorthy, Stein, McBrairty, Al-Hashimi (bb0675) 2015 Tolman, Flanagan, Kennedy, Prestegard (bb0405) 1997; 4 Bhattacharyya, Key, Chen, Best, Hollenkamp, Grey (bb0770) 2010; 9 Sabo, Trent, Lee (bb0640) 2015; 24 Tolman, Ruan (bb0390) 2006; 106 Lipari, Szabo (bb0155) 1982; 104 Hyberts, Milbradt, Wagner, Arthanari, Wagner (bb0985) 2012; 52 Kazimierczuk, Orekhov (bb0970) 2011; 50 Palmer (bb0125) 2003; 30 Sharaf, Barnes, Charlton, Young, Pielak (bb1380) 2010; 202 Wand (bb0305) 2001; 8 Smith, Zhou, Gorensek, Senske, Pielak (bb1290) 2016; 113 Rezaei-Ghaleh, Klama, Munari, Zweckstetter (bb0240) 2013; 52 Ferrage, Cowburn, Ghose (bb0200) 2009; 131 Fenwick, Esteban-Martín, Richter, Lee, Walter, Milovanovic, Becker, Lakomek, Griesinger, Salvatella (bb0590) 2011; 133 Clore, Iwahara (bb1035) 2009; 109 Tjandra, Bax (bb1000) 1997; 278 Markwick, Bouvignies, Blackledge (bb0490) 2007; 129 Vallurupalli, Hansen, Stollar, Meirovitch, Kay (bb0690) 2007; 104 Teague (bb0090) 2003; 2 Al-Hashimi, Gosser, Gorin, Hu, Majumdar, Patel (bb0450) 2002; 315 Schmidt, Guntert (bb1330) 2012; 134 Duchardt, Richter, Ohlenschlager, Gorlach, Wohnert, Schwalbe (bb0565) 2004; 126 Modig, Poulsen (bb0290) 2008; 42 Eichmüller, Skrynnikov (bb0635) 2005; 32 Boisbouvier, Brutscher, Pardi, Marion, Simorre (bb0580) 2000; 122 Yamaguchi, Yagi, Kato (bb0805) 2017 Laue, Mayger, Skilling, Staunton (bb0920) 1986; 68 Gaponenko, Sarma, Altieri, Horita, Li, Byrd (bb1015) 2004; 28 Klein-Seetharaman, Oikawa, Grimshaw, Wirmer, Duchardt, Ueda, Imoto, Smith, Dobson, Schwalbe (bb0280) 2002; 295 Ying, Delaglio, Torchia, Bax (bb0995) 2017; 68 Religa, Ruschak, Rosenzweig, Kay (bb1145) 2011; 133 Ye, Liu, Xu, Liu, Li (bb1350) 2015; 54 Nikolova, Kim, Wise, O'Brien, Andricioaei, Al-Hashimi (bb0680) 2011; 470 Gelis, Bonvin, Keramisanou, Koukaki, Gouridis, Karamanou, Economou, Kalodimos (bb1115) 2007; 131 Wang, Li, Pielak (bb1270) 2010; 132 Sakakibara, Sasaki, Ikeya, Hamatsu, Hanashima, Mishima, Yoshimasu, Hayashi, Mikawa, Walchli, Smith, Shirakawa, Guntert, Ito (bb1315) 2009; 458 Fiala, Spackova, Foldynova-Trantirkova, Sponer, Sklenar, Trantirek (bb0570) 2011; 133 Jaravine, Ibraghimov, Orekhov (bb0945) 2006; 3 Takeda, Miyanoiri, Terauchi, Kainosho (bb0875) 2016; 66 Religa, Sprangers, Kay (bb1135) 2010; 328 Fenwick, Schwieters, Vögeli (bb0595) 2016; 138 Velyvis, Ruschak, Kay (bb0830) 2012; 7 Serber, Keatinge-Clay, Ledwidge, Kelly, Miller, Dötsch (bb1165) 2001; 123 Danielsson, Mu, Lang, Wang, Binolfi, Theillet, Bekei, Logan, Selenko, Wennerstrom, Oliveberg (bb1225) 2015; 112 Guntert (bb1110) 2009; 38 Latham, Kay (bb1305) 2013; 55 Chakrabarti, Ban, Pratihar, Reddy, Becker, Griesinger, Lee (bb0730) 2016; 269 Bouvignies, Bernadó, Meier, Cho, Grzesiek, Brüschweiler, Blackledge (bb0435) 2005; 102 Schwieters, Clore (bb0445) 2007; 46 Venkatesan, Rual, Vazquez, Stelzl, Lemmens, Hirozane-Kishikawa, Hao, Zenkner, Xin, Goh, Yildirim, Simonis, Heinzmann, Gebreab, Sahalie, Cevik, Simon, de Smet, Dann, Smolyar, Vinayagam, Yu, Szeto, Borick, Dricot, Klitgord, Murray, Lin, Lalowski, Timm, Rau, Boone, Braun, Cusick, Roth, Hill, Tavernier, W Opitz (10.1016/j.bbagen.2017.08.020_bb0795) 2015; 62 Xue (10.1016/j.bbagen.2017.08.020_bb0330) 2012; 134 Rosenzweig (10.1016/j.bbagen.2017.08.020_bb1085) 2013; 339 Bax (10.1016/j.bbagen.2017.08.020_bb0395) 1994; 239 Fenwick (10.1016/j.bbagen.2017.08.020_bb0590) 2011; 133 Yagi (10.1016/j.bbagen.2017.08.020_bb1365) 2013; 21 Arkin (10.1016/j.bbagen.2017.08.020_bb0035) 2014; 21 Carlomagno (10.1016/j.bbagen.2017.08.020_bb0585) 1999; 121 Tugarinov (10.1016/j.bbagen.2017.08.020_bb0400) 2005; 102 Chen (10.1016/j.bbagen.2017.08.020_bb1030) 2012; 326 Karplus (10.1016/j.bbagen.2017.08.020_bb0115) 2005; 102 Loria (10.1016/j.bbagen.2017.08.020_bb0045) 2008; 41 Wang (10.1016/j.bbagen.2017.08.020_bb1270) 2010; 132 Ayala (10.1016/j.bbagen.2017.08.020_bb0825) 2009; 43 Lakomek (10.1016/j.bbagen.2017.08.020_bb0190) 2012; 53 Lindorff-Larsen (10.1016/j.bbagen.2017.08.020_bb0335) 2016; 120 Ban (10.1016/j.bbagen.2017.08.020_bb0630) 2011; 50 Neudecker (10.1016/j.bbagen.2017.08.020_bb0625) 2006; 34 Ellis (10.1016/j.bbagen.2017.08.020_bb1260) 2001; 26 Motlagh (10.1016/j.bbagen.2017.08.020_bb0050) 2014; 508 Kazimierczuk (10.1016/j.bbagen.2017.08.020_bb0970) 2011; 50 Mueller (10.1016/j.bbagen.2017.08.020_bb1075) 2000; 300 Vögeli (10.1016/j.bbagen.2017.08.020_bb0520) 2009; 131 Guntert (10.1016/j.bbagen.2017.08.020_bb1110) 2009; 38 Latham (10.1016/j.bbagen.2017.08.020_bb1310) 2014; 426 Velyvis (10.1016/j.bbagen.2017.08.020_bb1155) 2013; 135 Beck (10.1016/j.bbagen.2017.08.020_bb1375) 2011; 7 Guijarro (10.1016/j.bbagen.2017.08.020_bb0765) 1998; 276 Abyzov (10.1016/j.bbagen.2017.08.020_bb0270) 2016; 138 Chiarparin (10.1016/j.bbagen.2017.08.020_bb0530) 2000; 122 Bremi (10.1016/j.bbagen.2017.08.020_bb0430) 1997; 119 Lee (10.1016/j.bbagen.2017.08.020_bb0180) 1998; 9 Hoch (10.1016/j.bbagen.2017.08.020_bb0925) 2014; 47 Vallurupalli (10.1016/j.bbagen.2017.08.020_bb0690) 2007; 104 Frauenfelder (10.1016/j.bbagen.2017.08.020_bb0060) 1991; 254 Xue (10.1016/j.bbagen.2017.08.020_bb0675) 2015 Liu (10.1016/j.bbagen.2017.08.020_bb1210) 2009; 462 Meiler (10.1016/j.bbagen.2017.08.020_bb0410) 2001; 123 Korzhnev (10.1016/j.bbagen.2017.08.020_bb0665) 2009; 386 Ye (10.1016/j.bbagen.2017.08.020_bb1350) 2015; 54 Zhou (10.1016/j.bbagen.2017.08.020_bb1275) 2008; 37 Balbach (10.1016/j.bbagen.2017.08.020_bb0755) 1995; 2 Sekhar (10.1016/j.bbagen.2017.08.020_bb0030) 2013; 110 Bax (10.1016/j.bbagen.2017.08.020_bb0385) 2001 Yamaguchi (10.1016/j.bbagen.2017.08.020_bb0340) 2014; 53 Hamelberg (10.1016/j.bbagen.2017.08.020_bb0480) 2004; 120 Rajesh (10.1016/j.bbagen.2017.08.020_bb0845) 2003; 27 Palmer (10.1016/j.bbagen.2017.08.020_bb0655) 2006; 106 Harada (10.1016/j.bbagen.2017.08.020_bb1280) 2012; 134 Korzhnev (10.1016/j.bbagen.2017.08.020_bb0195) 2002; 124 Reif (10.1016/j.bbagen.2017.08.020_bb0510) 1997; 276 Barnes (10.1016/j.bbagen.2017.08.020_bb1295) 2011; 12 Clore (10.1016/j.bbagen.2017.08.020_bb0175) 1990; 112 Berjanskii (10.1016/j.bbagen.2017.08.020_bb0370) 2013; 135 Haupt (10.1016/j.bbagen.2017.08.020_bb0740) 2011; 133 Frederick (10.1016/j.bbagen.2017.08.020_bb0315) 2007; 448 Pervushin (10.1016/j.bbagen.2017.08.020_bb0220) 1997; 94 Barna (10.1016/j.bbagen.2017.08.020_bb0905) 1987; 73 Clore (10.1016/j.bbagen.2017.08.020_bb1020) 1998; 120 Sprangers (10.1016/j.bbagen.2017.08.020_bb1125) 2007; 445 Rezaei-Ghaleh (10.1016/j.bbagen.2017.08.020_bb0240) 2013; 52 Kato (10.1016/j.bbagen.2017.08.020_bb0800) 2010; 56 Gardner (10.1016/j.bbagen.2017.08.020_bb0815) 1997; 119 Zeeb (10.1016/j.bbagen.2017.08.020_bb0745) 2004; 34 Brocchieri (10.1016/j.bbagen.2017.08.020_bb1080) 2005; 33 Tugarinov (10.1016/j.bbagen.2017.08.020_bb1065) 2005; 102 Religa (10.1016/j.bbagen.2017.08.020_bb1145) 2011; 133 Mobli (10.1016/j.bbagen.2017.08.020_bb0900) 2006; 182 Modig (10.1016/j.bbagen.2017.08.020_bb0290) 2008; 42 Sinha (10.1016/j.bbagen.2017.08.020_bb0820) 2011; 50 Smith (10.1016/j.bbagen.2017.08.020_bb0645) 2016; 113 Latham (10.1016/j.bbagen.2017.08.020_bb1305) 2013; 55 Muntener (10.1016/j.bbagen.2017.08.020_bb1235) 2016; 7 Mitrea (10.1016/j.bbagen.2017.08.020_bb0230) 2016; 5 Forsén (10.1016/j.bbagen.2017.08.020_bb0710) 1963; 39 Tolman (10.1016/j.bbagen.2017.08.020_bb0415) 2002; 124 Vallurupalli (10.1016/j.bbagen.2017.08.020_bb0705) 2012; 134 Schmidt (10.1016/j.bbagen.2017.08.020_bb1330) 2012; 134 Matsuki (10.1016/j.bbagen.2017.08.020_bb0955) 2009; 131 Iwahara (10.1016/j.bbagen.2017.08.020_bb1005) 2004; 126 Khan (10.1016/j.bbagen.2017.08.020_bb0260) 2015; 109 Bekei (10.1016/j.bbagen.2017.08.020_bb1200) 2013 Hamatsu (10.1016/j.bbagen.2017.08.020_bb0935) 2013; 135 Tugarinov (10.1016/j.bbagen.2017.08.020_bb1070) 2004; 126 Keskin (10.1016/j.bbagen.2017.08.020_bb0070) 2007; 7 Baldwin (10.1016/j.bbagen.2017.08.020_bb0660) 2010; 132 Hansel (10.1016/j.bbagen.2017.08.020_bb1230) 2009; 131 Fawzi (10.1016/j.bbagen.2017.08.020_bb0725) 2014; 53 Ikeya (10.1016/j.bbagen.2017.08.020_bb1325) 2011; 50 Stern (10.1016/j.bbagen.2017.08.020_bb0980) 2007; 188 Ying (10.1016/j.bbagen.2017.08.020_bb0995) 2017; 68 Luginbuhl (10.1016/j.bbagen.2017.08.020_bb0130) 2002; 40 Muhandiram (10.1016/j.bbagen.2017.08.020_bb0300) 1995; 117 Miklos (10.1016/j.bbagen.2017.08.020_bb1265) 2010; 49 Brüschweiler (10.1016/j.bbagen.2017.08.020_bb0425) 1994; 116 Yang (10.1016/j.bbagen.2017.08.020_bb0550) 1998; 276 Kazimierczuk (10.1016/j.bbagen.2017.08.020_bb0915) 2008; 192 Kay (10.1016/j.bbagen.2017.08.020_bb0150) 1989; 28 Korzhnev (10.1016/j.bbagen.2017.08.020_bb0185) 1997; 127 Gelis (10.1016/j.bbagen.2017.08.020_bb1115) 2007; 131 Theillet (10.1016/j.bbagen.2017.08.020_bb1190) 2016; 530 Lipari (10.1016/j.bbagen.2017.08.020_bb0155) 1982; 104 Duchardt (10.1016/j.bbagen.2017.08.020_bb0565) 2004; 126 Farber (10.1016/j.bbagen.2017.08.020_bb0670) 2015; 7 Chakrabarti (10.1016/j.bbagen.2017.08.020_bb0730) 2016; 269 Jensen (10.1016/j.bbagen.2017.08.020_bb0505) 2009; 17 Anthis (10.1016/j.bbagen.2017.08.020_bb0700) 2015; 48 Danielsson (10.1016/j.bbagen.2017.08.020_bb1225) 2015; 112 Schanda (10.1016/j.bbagen.2017.08.020_bb0780) 2005; 127 Linnet (10.1016/j.bbagen.2017.08.020_bb0965) 2016; 64 Yang (10.1016/j.bbagen.2017.08.020_bb0310) 1996; 263 Kainosho (10.1016/j.bbagen.2017.08.020_bb0865) 2006; 440 Ma (10.1016/j.bbagen.2017.08.020_bb0465) 1999; 12 Teague (10.1016/j.bbagen.2017.08.020_bb0090) 2003; 2 Klein-Seetharaman (10.1016/j.bbagen.2017.08.020_bb0280) 2002; 295 Hikone (10.1016/j.bbagen.2017.08.020_bb1355) 2016; 66 Tzeng (10.1016/j.bbagen.2017.08.020_bb0085) 2013; 9 Xue (10.1016/j.bbagen.2017.08.020_bb0285) 2009; 18 Schwieters (10.1016/j.bbagen.2017.08.020_bb0445) 2007; 46 Pervushin (10.1016/j.bbagen.2017.08.020_bb0880) 1997; 94 Hyberts (10.1016/j.bbagen.2017.08.020_bb0930) 2007; 129 Smith (10.1016/j.bbagen.2017.08.020_bb0040) 2008; 130 Zhang (10.1016/j.bbagen.2017.08.020_bb1285) 1995; 34 Kubo (10.1016/j.bbagen.2017.08.020_bb1345) 2013; 52 Hammes (10.1016/j.bbagen.2017.08.020_bb0460) 2009; 106 Libich (10.1016/j.bbagen.2017.08.020_bb0720) 2015; 112 Glaeser (10.1016/j.bbagen.2017.08.020_bb0010) 2016; 13 Leung (10.1016/j.bbagen.2017.08.020_bb0350) 2014; 23 Tzeng (10.1016/j.bbagen.2017.08.020_bb0325) 2012; 488 Beck (10.1016/j.bbagen.2017.08.020_bb1370) 1979; 97 Grishaev (10.1016/j.bbagen.2017.08.020_bb1045) 2005; 127 Hembram (10.1016/j.bbagen.2017.08.020_bb1245) 2013; 438 Fenwick (10.1016/j.bbagen.2017.08.020_bb0595) 2016; 138 Velyvis (10.1016/j.bbagen.2017.08.020_bb0830) 2012; 7 Al-Hashimi (10.1016/j.bbagen.2017.08.020_bb0450) 2002; 315 Clore (10.1016/j.bbagen.2017.08.020_bb1035) 2009; 109 Ban (10.1016/j.bbagen.2017.08.020_bb0735) 2013; 57 Grishaev (10.1016/j.bbagen.2017.08.020_bb1055) 2008; 40 Nobeli (10.1016/j.bbagen.2017.08.020_bb0025) 2009; 27 Brüschweiler (10.1016/j.bbagen.2017.08.020_bb0245) 1995; 268 Pelupessy (10.1016/j.bbagen.2017.08.020_bb0545) 1999; 14 Pelupessy (10.1016/j.bbagen.2017.08.020_bb0515) 2003; 25 Theillet (10.1016/j.bbagen.2017.08.020_bb0255) 2014; 114 Saio (10.1016/j.bbagen.2017.08.020_bb1120) 2014; 344 Ruschak (10.1016/j.bbagen.2017.08.020_bb1150) 2012; 109 Matsuki (10.1016/j.bbagen.2017.08.020_bb0960) 2011; 115 Bertini (10.1016/j.bbagen.2017.08.020_bb1010) 2005; 6 Schwalbe (10.1016/j.bbagen.2017.08.020_bb0275) 1997 Nicholson (10.1016/j.bbagen.2017.08.020_bb0295) 1992; 31 Bhakdi (10.1016/j.bbagen.2017.08.020_bb1255) 1993; 182 Korzhnev (10.1016/j.bbagen.2017.08.020_bb0610) 2008; 41 Gasper (10.1016/j.bbagen.2017.08.020_bb0495) 2012; 109 Palmer (10.1016/j.bbagen.2017.08.020_bb0210) 2004; 104 Tolman (10.1016/j.bbagen.2017.08.020_bb0405) 1997; 4 Shen (10.1016/j.bbagen.2017.08.020_bb1360) 2008; 105 Venditti (10.1016/j.bbagen.2017.08.020_bb1060) 2015; 112 Douglas (10.1016/j.bbagen.2017.08.020_bb1025) 2007; 104 Rosen (10.1016/j.bbagen.2017.08.020_bb0810) 1996; 263 Sun (10.1016/j.bbagen.2017.08.020_bb0990) 2015; 62 Yang (10.1016/j.bbagen.2017.08.020_bb0870) 2015; 54 Smith (10.1016/j.bbagen.2017.08.020_bb1300) 2015; 24 Hyberts (10.1016/j.bbagen.2017.08.020_bb0910) 2010; 132 Serber (10.1016/j.bbagen.2017.08.020_bb1165) 2001; 123 Inomata (10.1016/j.bbagen.2017.08.020_bb1195) 2009; 458 Boehr (10.1016/j.bbagen.2017.08.020_bb0065) 2009; 5 Gill (10.1016/j.bbagen.2017.08.020_bb0265) 2016; 18 Palmer (10.1016/j.bbagen.2017.08.020_bb0125) 2003; 30 Zhang (10.1016/j.bbagen.2017.08.020_bb0345) 2007; 450 Nikolova (10.1016/j.bbagen.2017.08.020_bb0680) 2011; 470 Latham (10.1016/j.bbagen.2017.08.020_bb1160) 2014; 111 Yamaguchi (10.1016/j.bbagen.2017.08.020_bb0805) 2017 Banci (10.1016/j.bbagen.2017.08.020_bb1205) 2013; 9 Case (10.1016/j.bbagen.2017.08.020_bb0365) 2013; 23 Salmon (10.1016/j.bbagen.2017.08.020_bb0455) 2013; 135 Koehler (10.1016/j.bbagen.2017.08.020_bb1215) 2011; 59 Bouvignies (10.1016/j.bbagen.2017.08.020_bb0435) 2005; 102 Pelupessy (10.1016/j.bbagen.2017.08.020_bb0540) 1999; 13 Laue (10.1016/j.bbagen.2017.08.020_bb0920) 1986; 68 Lakomek (10.1016/j.bbagen.2017.08.020_bb0250) 2008; 41 Bowen (10.1016/j.bbagen.2017.08.020_bb0785) 2008; 47 Smith (10.1016/j.bbagen.2017.08.020_bb0605) 2015; 54 Markwick (10.1016/j.bbagen.2017.08.020_bb0485) 2009; 131 Selenko (10.1016/j.bbagen.2017.08.020_bb1175) 2006; 103 Igumenova (10.1016/j.bbagen.2017.08.020_bb0695) 2007; 129 Korzhnev (10.1016/j.bbagen.2017.08.020_bb0650) 2010; 329 Bhattacharyya ( |
| References_xml | – start-page: 1 year: 1997 end-page: 15 ident: bb0275 article-title: structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 publication-title: Biochemistry – volume: 113 start-page: E6939 year: 2016 end-page: E6945 ident: bb0105 article-title: Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy publication-title: Proc. Natl. Acad. Sci. – volume: 386 start-page: 391 year: 2009 end-page: 405 ident: bb0665 article-title: Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy publication-title: J. Mol. Biol. – volume: 33 start-page: 3390 year: 2005 end-page: 3400 ident: bb1080 article-title: Protein length in eukaryotic and prokaryotic proteomes publication-title: Nucleic Acids Res. – volume: 37 start-page: 225 year: 2007 end-page: 229 ident: bb0790 article-title: Improving cell-free protein synthesis for stable-isotope labeling publication-title: J. Biomol. NMR – volume: 438 start-page: 653 year: 2013 end-page: 659 ident: bb1245 article-title: An in-cell NMR study of monitoring stress-induced increase of cytosolic Ca2 publication-title: Biochem. Biophys. Res. Commun. – volume: 134 start-page: 6365 year: 2012 end-page: 6374 ident: bb0380 article-title: Interpreting protein structural dynamics from NMR chemical shifts publication-title: J. Am. Chem. Soc. – volume: 9 start-page: 297 year: 2013 end-page: 299 ident: bb1205 article-title: Atomic-resolution monitoring of protein maturation in live human cells by NMR publication-title: Nat. Chem. Biol. – volume: 132 year: 2010 ident: bb0910 article-title: Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR data publication-title: J. Am. Chem. Soc. – volume: 295 start-page: 1719 year: 2002 end-page: 1722 ident: bb0280 article-title: Long-range interactions within a nonnative protein publication-title: Science – volume: 36 start-page: 179 year: 2006 end-page: 188 ident: bb1180 article-title: In-cell NMR spectroscopy of proteins inside publication-title: J. Biomol. NMR – volume: 53 start-page: 209 year: 2012 end-page: 221 ident: bb0190 article-title: Measurement of 15N relaxation rates in perdeuterated proteins by TROSY-based methods publication-title: J. Biomol. NMR – volume: 124 start-page: 10743 year: 2002 end-page: 10753 ident: bb0195 article-title: An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates publication-title: J. Am. Chem. Soc. – volume: 126 start-page: 5879 year: 2004 end-page: 5896 ident: bb1005 article-title: Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule publication-title: J. Am. Chem. Soc. – volume: 326 start-page: 47 year: 2012 end-page: 67 ident: bb1030 article-title: The use of residual dipolar coupling in studying proteins by NMR publication-title: Top. Curr. Chem. – volume: 23 start-page: 172 year: 2013 end-page: 176 ident: bb0365 article-title: Chemical shifts in biomolecules publication-title: Curr. Opin. Struct. Biol. – volume: 5 year: 2016 ident: bb0230 article-title: Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA publication-title: elife – volume: 127 start-page: 14970 year: 2005 end-page: 14971 ident: bb0375 article-title: A simple method to predict protein flexibility using secondary chemical shifts publication-title: J. Am. Chem. Soc. – volume: 15 start-page: 241 year: 1999 end-page: 250 ident: bb0555 article-title: Determination of sugar conformation in large RNA oligonucleotides from analysis of dipole–dipole cross correlated relaxation by solution NMR spectroscopy publication-title: J. Biomol. NMR – volume: 67 start-page: 23 year: 2017 end-page: 34 ident: bb0860 article-title: Bacterial production of site specific 13C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins publication-title: J. Biomol. NMR – volume: 134 start-page: 2555 year: 2012 end-page: 2562 ident: bb0330 article-title: Microsecond time-scale conformational exchange in proteins: using long molecular dynamics trajectory to simulate NMR relaxation dispersion data publication-title: J. Am. Chem. Soc. – volume: 448 start-page: 325 year: 2007 end-page: 329 ident: bb0315 article-title: Conformational entropy in molecular recognition by proteins publication-title: Nature – volume: 53 start-page: 10941 year: 2014 end-page: 10944 ident: bb0340 article-title: Exploration of conformational spaces of high-mannose-type oligosaccharides by an NMR-validated simulation publication-title: Angew. Chem. Int. Ed. Eng. – volume: 134 start-page: 4842 year: 2012 end-page: 4849 ident: bb1280 article-title: Protein crowding affects hydration structure and dynamics publication-title: J. Am. Chem. Soc. – volume: 42 start-page: 163 year: 2008 end-page: 177 ident: bb0290 article-title: Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP publication-title: J. Biomol. NMR – volume: 5 start-page: 789 year: 2009 end-page: 796 ident: bb0065 article-title: The role of dynamic conformational ensembles in biomolecular recognition publication-title: Nat. Chem. Biol. – volume: 26 start-page: 597 year: 2001 end-page: 604 ident: bb1260 article-title: Macromolecular crowding: obvious but underappreciated publication-title: Trends Biochem. Sci. – volume: 508 start-page: 331 year: 2014 end-page: 339 ident: bb0050 article-title: The ensemble nature of allostery publication-title: Nature – volume: 112 start-page: 4989 year: 1990 end-page: 4991 ident: bb0175 article-title: Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins publication-title: J. Am. Chem. Soc. – volume: 254 start-page: 1598 year: 1991 end-page: 1603 ident: bb0060 article-title: The energy landscapes and motions of proteins publication-title: Science – volume: 207 start-page: 294 year: 2010 end-page: 303 ident: bb0205 article-title: On the measurement of publication-title: J. Magn. Reson. – volume: 699 year: 2016 ident: bb1335 article-title: Protein NMR structure refinement based on Bayesian inference publication-title: J. Phys. Conf. Ser. – volume: 106 start-page: 1700 year: 2006 end-page: 1719 ident: bb0655 article-title: Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy publication-title: Chem. Rev. – volume: 263 start-page: 627 year: 1996 end-page: 636 ident: bb0810 article-title: Selective methyl group protonation of perdeuterated proteins publication-title: J. Mol. Biol. – volume: 299 start-page: 1362 year: 2003 end-page: 1367 ident: bb0080 article-title: Antibody multispecificity mediated by conformational diversity publication-title: Science – volume: 131 start-page: 9239 year: 2009 end-page: 9249 ident: bb0775 article-title: Real-time NMR investigations of structural changes in silicon electrodes for lithium-ion batteries publication-title: J. Am. Chem. Soc. – volume: 27 start-page: 81 year: 2003 end-page: 86 ident: bb0845 article-title: A novel method for the biosynthesis of deuterated proteins with selective protonation at the aromatic rings of Phe, Tyr and Trp publication-title: J. Biomol. NMR – volume: 120 start-page: 7905 year: 1998 end-page: 7915 ident: bb0215 article-title: Longitudinal and transverse 1H-15N dipolar/15N chemical shift anisotropy relaxation interference: unambiguous determination of rotational diffusion tensors and chemical Exchane effects in biological macromolecules publication-title: J. Am. Chem. Soc. – volume: 300 start-page: 197 year: 2000 end-page: 212 ident: bb1075 article-title: Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein publication-title: J. Mol. Biol. – volume: 51 start-page: 57 year: 2011 end-page: 70 ident: bb0615 article-title: The feasibility of parameterizing four-state equilibria using relaxation dispersion measurements publication-title: J. Biomol. NMR – volume: 126 start-page: 9827 year: 2004 end-page: 9836 ident: bb1070 article-title: Stereospecific NMR assignments of prochiral methyls, rotameric states and dynamics of valine residues in malate synthase G publication-title: J. Am. Chem. Soc. – volume: 38 start-page: 197 year: 2001 end-page: 266 ident: bb0145 article-title: NMR studies of Brownian tumbling and internal motions in proteins publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 135 start-page: 1688 year: 2013 end-page: 1691 ident: bb0935 article-title: High-resolution heteronuclear multidimensional NMR of proteins in living insect cells using a baculovirus protein expression system publication-title: J. Am. Chem. Soc. – volume: 122 start-page: 12728 year: 2000 end-page: 12731 ident: bb0560 article-title: NMR spectroscopic determination of angles α and ζ in RNA from CH-dipolar coupling, P-CSA cross-correlated relaxation publication-title: J. Am. Chem. Soc. – volume: 458 start-page: 102 year: 2009 end-page: 105 ident: bb1315 article-title: Protein structure determination in living cells by in-cell NMR spectroscopy publication-title: Nature – volume: 46 start-page: 1152 year: 2007 end-page: 1166 ident: bb0445 article-title: A physical picture of atomic motions within the Dickerson DNA dodecamer in solution derived from joint ensemble refinement against NMR and large-angle X-ray scattering data publication-title: Biochemistry – volume: 68 start-page: 101 year: 2017 end-page: 118 ident: bb0995 article-title: Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data publication-title: J. Biomol. NMR – volume: 50 start-page: 10189 year: 2011 end-page: 10191 ident: bb0820 article-title: Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes publication-title: Biochemistry – volume: 458 start-page: 106 year: 2009 end-page: 109 ident: bb1195 article-title: High-resolution multi-dimensional NMR spectroscopy of proteins in human cells publication-title: Nature – volume: 7 start-page: 2821 year: 2016 end-page: 2825 ident: bb1235 article-title: In-cell protein structures from 2D NMR experiments publication-title: J. Phys. Chem. Lett. – volume: 9 start-page: 287 year: 1998 end-page: 298 ident: bb0180 article-title: Rotational diffusion anisotropy of proteins from simultaneous analysis of publication-title: J. Biomol. NMR – volume: 131 start-page: 6048 year: 2009 end-page: 6049 ident: bb0200 article-title: Accurate sampling of high-frequency motions in proteins by steady-state 15N publication-title: J. Am. Chem. Soc. – volume: 34 start-page: 129 year: 2006 end-page: 135 ident: bb0625 article-title: Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain publication-title: J. Biomol. NMR – volume: 116 start-page: 6424 year: 2016 end-page: 6462 ident: bb0120 article-title: Dynamic protein interaction networks and new structural paradigms in signaling publication-title: Chem. Rev. – volume: 52 start-page: 1208 year: 2013 end-page: 1211 ident: bb1345 article-title: A gel-encapsulated bioreactor system for NMR studies of protein-protein interactions in living mammalian cells publication-title: Angew. Chem. Int. Ed. Eng. – volume: 202 start-page: 140 year: 2010 end-page: 146 ident: bb1380 article-title: A bioreactor for in-cell protein NMR publication-title: J. Magn. Reson. – volume: 94 start-page: 12366 year: 1997 end-page: 12371 ident: bb0220 article-title: Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 39 start-page: 2892 year: 1963 end-page: 2901 ident: bb0710 article-title: Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance publication-title: J. Chem. Phys. – volume: 40 start-page: 1339 year: 2011 end-page: 1355 ident: bb0470 article-title: Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles publication-title: Eur. Biophys. J. – volume: 104 start-page: 4559 year: 1982 end-page: 4570 ident: bb0155 article-title: Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results publication-title: J. Am. Chem. Soc. – volume: 112 start-page: 11565 year: 2015 end-page: 11570 ident: bb1060 article-title: Dynamic equilibrium between closed and partially closed states of the bacterial enzyme I unveiled by solution NMR and X-ray scattering publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 537 start-page: 202 year: 2016 end-page: 206 ident: bb1100 article-title: Structural basis for the antifolding activity of a molecular chaperone publication-title: Nature – volume: 124 start-page: 12020 year: 2002 end-page: 12030 ident: bb0415 article-title: A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy publication-title: J. Am. Chem. Soc. – volume: 104 start-page: 3623 year: 2004 end-page: 3640 ident: bb0210 article-title: NMR characterization of the dynamics of biomacromolecules publication-title: Chem. Rev. – volume: 135 start-page: 14536 year: 2013 end-page: 14539 ident: bb0370 article-title: A simple method to measure protein side-chain mobility using NMR chemical shifts publication-title: J. Am. Chem. Soc. – volume: 52 start-page: 3911 year: 2013 end-page: 3915 ident: bb0235 article-title: Internal dynamics of the homotrimeric HIV-1 viral coat protein gp41 on multiple time scales publication-title: Angew. Chem. Int. Ed. – volume: 134 start-page: 8148 year: 2012 end-page: 8161 ident: bb0705 article-title: Studying “invisible” excited protein states in slow exchange with a major state conformation publication-title: J. Am. Chem. Soc. – volume: 8 start-page: 926 year: 2001 end-page: 931 ident: bb0305 article-title: Dynamic activation of protein function: a view emerging from NMR spectroscopy publication-title: Nat. Struct. Biol. – volume: 122 start-page: 6779 year: 2000 end-page: 6780 ident: bb0580 article-title: NMR determination of sugar puckers in nucleic Acids from CSA publication-title: J. Am. Chem. Soc. – volume: 154 start-page: 157 year: 2002 end-page: 160 ident: bb0620 article-title: R1ρ relaxation outside of the fast-exchange limit publication-title: J. Magn. Reson. – volume: 62 start-page: 105 year: 2015 end-page: 117 ident: bb0990 article-title: Efficient and generalized processing of multidimensional NUS NMR data: the NESTA algorithm and comparison of regularization terms publication-title: J. Biomol. NMR – volume: 13 start-page: 28 year: 2016 end-page: 32 ident: bb0010 article-title: How good can cryo-EM become? publication-title: Nat. Methods – volume: 123 start-page: 2446 year: 2001 end-page: 2447 ident: bb1165 article-title: High-resolution macromolecular NMR spectroscopy inside living cells publication-title: J. Am. Chem. Soc. – volume: 129 start-page: 11468 year: 2007 end-page: 11479 ident: bb0170 article-title: An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange publication-title: J. Am. Chem. Soc. – volume: 131 start-page: 3668 year: 2009 end-page: 3678 ident: bb0520 article-title: Correlated dynamics between protein HN and HC bonds observed by NMR cross relaxation publication-title: J. Am. Chem. Soc. – volume: 117 start-page: 139 year: 2017 end-page: 155 ident: bb0110 article-title: GPCR dynamics: structures in motion publication-title: Chem. Rev. – volume: 54 start-page: 207 year: 2015 end-page: 210 ident: bb0605 article-title: Population shuffling of protein conformations publication-title: Angew. Chem. Int. Ed. Eng. – volume: 50 start-page: 11437 year: 2011 end-page: 11440 ident: bb0630 article-title: Kinetics of conformational sampling in ubiquitin publication-title: Angew. Chem. Int. Ed. Eng. – volume: 7 start-page: 191 year: 2015 end-page: 200 ident: bb0670 article-title: Relaxation dispersion NMR spectroscopy for the study of protein allostery publication-title: Biophys. Rev. – volume: 94 start-page: 12366 year: 1997 end-page: 12371 ident: bb0880 article-title: Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 104 start-page: 6644 year: 2007 end-page: 6648 ident: bb1025 article-title: DNA-nanotube-induced alignment of membrane proteins for NMR structure determination publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 50 start-page: 6548 year: 2011 end-page: 6551 ident: bb0975 article-title: Fast multidimensional NMR spectroscopy using compressed sensing publication-title: Angew. Chem. Int. Ed. Eng. – volume: 113 start-page: 1725 year: 2016 end-page: 1730 ident: bb1290 article-title: In-cell thermodynamics and a new role for protein surfaces publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 28 start-page: 205 year: 2004 end-page: 212 ident: bb1015 article-title: Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints publication-title: J. Biomol. NMR – volume: 131 start-page: 4648 year: 2009 end-page: 4656 ident: bb0955 article-title: Spectroscopy by integration of frequency and time domain information for fast acquisition of high-resolution dark spectra publication-title: J. Am. Chem. Soc. – volume: 138 start-page: 8412 year: 2016 end-page: 8421 ident: bb0595 article-title: Direct investigation of slow correlated dynamics in proteins via dipolar interactions publication-title: J. Am. Chem. Soc. – volume: 426 start-page: 3214 year: 2014 end-page: 3220 ident: bb1310 article-title: A similar in vitro and in cell lysate folding intermediate for the FF domain publication-title: J. Mol. Biol. – volume: 128 start-page: 9719 year: 2016 end-page: 9722 ident: bb0440 article-title: Kinetics of the antibody recognition site in the third IgG-binding domain of protein G publication-title: Angew. Chem. – volume: 56 start-page: 346 year: 2010 end-page: 359 ident: bb0800 article-title: Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 273 start-page: 283 year: 1997 end-page: 298 ident: bb1105 article-title: Torsion angle dynamics for NMR structure calculation with the new program DYANA publication-title: J. Mol. Biol. – volume: 55 start-page: 239 year: 2013 end-page: 247 ident: bb1305 article-title: Probing non-specific interactions of Ca(2)(+)-calmodulin in publication-title: J. Biomol. NMR – volume: 106 start-page: 1720 year: 2006 end-page: 1736 ident: bb0390 article-title: NMR residual dipolar couplings as probes of biomolecular dynamics publication-title: Chem. Rev. – volume: 182 start-page: 167 year: 1993 end-page: 175 ident: bb1255 article-title: A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes publication-title: Med. Microbiol. Immunol. – volume: 9 start-page: 1024 year: 2012 end-page: 1029 ident: bb1185 article-title: Interaction of alpha-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by (1)(9)F NMR publication-title: Mol. Pharm. – volume: 18 start-page: 5839 year: 2016 end-page: 5849 ident: bb0265 article-title: Dynamics of GCN4 facilitate DNA interaction: a model-free analysis of an intrinsically disordered region publication-title: Phys. Chem. Chem. Phys. – volume: 52 start-page: 10237 year: 2016 end-page: 10240 ident: bb1240 article-title: 3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy publication-title: Chem. Commun. (Camb.) – volume: 320 start-page: 1471 year: 2008 end-page: 1475 ident: bb0075 article-title: Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution publication-title: Science – volume: 127 start-page: 184 year: 1997 end-page: 191 ident: bb0185 article-title: Model-free Approach Beyond the Borders of its Applicability – volume: 344 start-page: 1250494 year: 2014 ident: bb1120 article-title: Structural basis for protein antiaggregation activity of the trigger factor chaperone publication-title: Science – volume: 462 start-page: 151 year: 2009 end-page: 175 ident: bb1210 article-title: Chapter 8 Segmental Isotopic Labeling of Proteins for Nuclear Magnetic Resonance – volume: 59 start-page: 360 year: 2011 end-page: 389 ident: bb1215 article-title: Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 263 start-page: 369 year: 1996 end-page: 382 ident: bb0310 article-title: Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding publication-title: J. Mol. Biol. – volume: 121 start-page: 1956 year: 1999 end-page: 1957 ident: bb0575 article-title: Determination of RNA sugar pucker mode from cross-correlated relaxation in solution NMR spectroscopy publication-title: J. Am. Chem. Soc. – volume: 35 start-page: 313 year: 2006 end-page: 327 ident: bb1050 article-title: A target function for quaternary structural refinement from small angle scattering and NMR orientational restraints publication-title: Eur. Biophys. J. – volume: 4 start-page: 292 year: 1997 end-page: 297 ident: bb0405 article-title: NMR evidence for slow collective motions in cyanometmyoglobin publication-title: Nat. Struct. Mol. Biol. – volume: 69 start-page: 726 year: 2007 end-page: 733 ident: bb1095 article-title: HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets publication-title: Proteins – volume: 49 start-page: 6984 year: 2010 end-page: 6991 ident: bb1265 article-title: Volume exclusion and soft interaction effects on protein stability under crowded conditions publication-title: Biochemistry – start-page: 194 year: 2017 end-page: 205 ident: bb0805 article-title: Stable isotope labeling of glycoproteins for NMR study publication-title: NMR in Glycoscience and Glycotechnology – volume: 276 start-page: 657 year: 1998 end-page: 667 ident: bb0765 article-title: Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy publication-title: J. Mol. Biol. – volume: 6 start-page: 83 year: 2009 end-page: 90 ident: bb0005 article-title: An empirical framework for binary interactome mapping publication-title: Nat. Methods – volume: 7 year: 2012 ident: bb0830 article-title: An economical method for production of (2)H, (13)CH3-threonine for solution NMR studies of large protein complexes: application to the 670 publication-title: PLoS One – volume: 125 start-page: 10420 year: 2003 end-page: 10428 ident: bb0895 article-title: Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes publication-title: J. Am. Chem. Soc. – volume: 41 start-page: 139 year: 2008 end-page: 155 ident: bb0250 article-title: Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics publication-title: J. Biomol. NMR – volume: 34 start-page: 65 year: 2004 end-page: 74 ident: bb0745 article-title: Protein folding studied by real-time NMR spectroscopy publication-title: Methods – volume: 126 start-page: 1962 year: 2004 end-page: 1970 ident: bb0565 article-title: Determination of the glycosidic bond angle chi in RNA from cross-correlated relaxation of CH dipolar coupling and N chemical shift anisotropy publication-title: J. Am. Chem. Soc. – volume: 4 start-page: 443 year: 1997 end-page: 450 ident: bb0160 article-title: Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy publication-title: Nat. Struct. Mol. Biol. – volume: 23 start-page: 1596 year: 2014 end-page: 1606 ident: bb0350 article-title: NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain publication-title: Protein Sci. – volume: 117 start-page: 11536 year: 1995 end-page: 11544 ident: bb0300 article-title: Measurement of 2H T1 and T1rho relaxation times in uniformly 13C-labeled and fractionally 2H-labeled proteins in solution publication-title: J. Am. Chem. Soc. – volume: 315 start-page: 95 year: 2002 end-page: 102 ident: bb0450 article-title: Concerted motions in HIV-1 TAR RNA may allow access to bound state conformations: RNA dynamics from NMR residual dipolar couplings publication-title: J. Mol. Biol. – volume: 121 start-page: 1945 year: 1999 end-page: 1948 ident: bb0585 article-title: Transferred cross-correlated relaxation: application to the determination of sugar pucker in an Aminoacylated tRNA-mimetic weakly bound to EF-Tu publication-title: J. Am. Chem. Soc. – volume: 130 start-page: 15361 year: 2008 end-page: 15373 ident: bb0040 article-title: Structural reorganization and preorganization in enzyme active sites: comparisons of experimental and theoretically ideal active site geometries in the multistep serine esterase reaction cycle publication-title: J. Am. Chem. Soc. – volume: 98 start-page: 7684 year: 2001 end-page: 7689 ident: bb0360 article-title: Functional dynamics in the active site of the ribonuclease binase publication-title: Proc. Natl. Acad. Sci. – year: 2001 ident: bb0385 article-title: Dipolar Couplings in Macromolecular Structure Determination – volume: 14 start-page: 818 year: 2013 end-page: 821 ident: bb0850 article-title: Selective isotope labelling of leucine residues by using alpha-ketoacid precursor compounds publication-title: Chembiochem – volume: 106 start-page: 13737 year: 2009 end-page: 13741 ident: bb0460 article-title: Conformational selection or induced fit: a flux description of reaction mechanism publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 64 start-page: 165 year: 2016 end-page: 173 ident: bb0965 article-title: Non-uniform sampling of NMR relaxation data publication-title: J. Biomol. NMR – volume: 35 start-page: 16843 year: 1996 end-page: 16851 ident: bb0750 article-title: Real-time refolding studies of 6-19F-tryptophan labeled Escherichia Coli dihydrofolate reductase using stopped-flow NMR spectroscopy publication-title: Biochemistry – volume: 239 start-page: 79 year: 1994 end-page: 105 ident: bb0395 article-title: Measurement of homo- and heteronuclear J couplings from quantitative J correlation publication-title: Methods Enzymol. – volume: 102 start-page: 622 year: 2005 end-page: 627 ident: bb0400 article-title: Solution NMR-derived Global Fold of a Monomeric 82-kDa Enzyme – volume: 125 start-page: 1731 year: 2003 end-page: 1737 ident: bb1090 article-title: HADDOCK: a protein-protein docking approach based on biochemical or biophysical information publication-title: J. Am. Chem. Soc. – volume: 52 start-page: 315 year: 2012 end-page: 327 ident: bb0985 article-title: Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional poisson gap scheduling publication-title: J. Biomol. NMR – volume: 131 start-page: 756 year: 2007 end-page: 769 ident: bb1115 article-title: Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR publication-title: Cell – volume: 112 start-page: 8817 year: 2015 end-page: 8823 ident: bb0720 article-title: Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 53 start-page: 10345 year: 2014 end-page: 10349 ident: bb0725 article-title: Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using 13C methyl-DEST and lifetime line broadening publication-title: Angew. Chem. Int. Ed. – volume: 21 start-page: 883 year: 2013 end-page: 890 ident: bb1365 article-title: Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites publication-title: Structure – volume: 450 start-page: 1263 year: 2007 end-page: 1267 ident: bb0345 article-title: Visualizing spatially correlated dynamics that directs RNA conformational transitions publication-title: Nature – volume: 47 start-page: 708 year: 2014 end-page: 717 ident: bb0925 article-title: Nonuniform sampling and maximum entropy reconstruction in multidimensional NMR publication-title: Acc. Chem. Res. – volume: 153 start-page: 293 year: 2013 end-page: 305 ident: bb0055 article-title: Allostery in disease and in drug discovery publication-title: Cell – volume: 102 start-page: 6679 year: 2005 end-page: 6685 ident: bb0115 article-title: Molecular dynamics and protein function publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 276 start-page: 939 year: 1998 end-page: 954 ident: bb0550 article-title: A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk publication-title: J. Mol. Biol. – volume: 530 start-page: 45 year: 2016 end-page: 50 ident: bb1190 article-title: Structural disorder of monomeric alpha-synuclein persists in mammalian cells publication-title: Nature – volume: 488 start-page: 236 year: 2012 end-page: 240 ident: bb0325 article-title: Protein activity regulation by conformational entropy publication-title: Nature – volume: 131 start-page: 16968 year: 2009 end-page: 16975 ident: bb0485 article-title: Toward a unified representation of protein structural dynamics in solution publication-title: J. Am. Chem. Soc. – volume: 7 start-page: 553 year: 2011 end-page: 559 ident: bb0475 article-title: Discovery of selective bioactive small molecules by targeting an RNA dynamic ensemble publication-title: Nat. Chem. Biol. – volume: 5 start-page: 1051 year: 2010 end-page: 1060 ident: bb1320 article-title: NMR protein structure determination in living publication-title: Nat. Protoc. – volume: 40 start-page: 199 year: 2002 end-page: 247 ident: bb0130 article-title: Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 16 start-page: 746 year: 2015 end-page: 751 ident: bb0855 article-title: Novel approaches in selective tryptophan isotope labeling by using publication-title: Chembiochem – volume: 48 start-page: 8023 year: 2009 end-page: 8031 ident: bb0500 article-title: Functional dynamics of the folded Ankyrin repeats of IκBα revealed by nuclear magnetic resonance publication-title: Biochemistry – volume: 50 start-page: 137 year: 2011 end-page: 146 ident: bb1325 article-title: Exclusively NOESY-based automated NMR assignment and structure determination of proteins publication-title: J. Biomol. NMR – volume: 57 start-page: 111 year: 2010 end-page: 158 ident: bb0140 article-title: Nuclear spin relaxation in isotropic and anisotropic media publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 66 start-page: 37 year: 2016 end-page: 53 ident: bb0875 article-title: C-13-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI) publication-title: J. Biomol. NMR – volume: 192 start-page: 123 year: 2008 end-page: 130 ident: bb0915 article-title: Optimization of random time domain sampling in multidimensional NMR publication-title: J. Magn. Reson. – volume: 339 start-page: 1080 year: 2013 end-page: 1083 ident: bb1085 article-title: Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction publication-title: Science – volume: 21 start-page: 1102 year: 2014 end-page: 1114 ident: bb0035 article-title: Small-molecule inhibitors of protein-protein interactions: progressing toward the reality publication-title: Chem. Biol. – volume: 18 start-page: 11904 year: 2013 end-page: 11937 ident: bb0165 article-title: Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy publication-title: Molecules (Basel, Switzerland) – volume: 138 start-page: 6240 year: 2016 end-page: 6251 ident: bb0270 article-title: Identification of dynamic modes in an intrinsically disordered protein using temperature-dependent NMR relaxation publication-title: J. Am. Chem. Soc. – volume: 276 start-page: 1230 year: 1997 end-page: 1233 ident: bb0510 article-title: Direct measurement of angles between bond vectors in high-resolution NMR publication-title: Science – volume: 43 start-page: 111 year: 2009 end-page: 119 ident: bb0825 article-title: An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein publication-title: J. Biomol. NMR – volume: 105 start-page: 4685 year: 2008 end-page: 4690 ident: bb1360 article-title: Consistent blind protein structure generation from NMR chemical shift data publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 440 start-page: 52 year: 2006 end-page: 57 ident: bb0865 article-title: Optimal isotope labelling for NMR protein structure determinations publication-title: Nature – volume: 8 start-page: 610 year: 2007 end-page: 612 ident: bb0840 article-title: Synthesis of a13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy publication-title: Chembiochem – volume: 470 start-page: 498 year: 2011 end-page: 502 ident: bb0680 article-title: Transient Hoogsteen base pairs in canonical duplex DNA publication-title: Nature – volume: 278 start-page: 1111 year: 1997 end-page: 1114 ident: bb1000 article-title: Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium publication-title: Science – volume: 221 start-page: 1 year: 2012 end-page: 4 ident: bb0600 article-title: Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead publication-title: J. Magn. Reson. – volume: 68 start-page: 14 year: 1986 end-page: 29 ident: bb0920 article-title: Reconstruction of phase sensitive 2D NMR spectra by maximum entropy publication-title: J. Magn. Reson. – volume: 12 start-page: 390 year: 2011 end-page: 391 ident: bb1295 article-title: Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy publication-title: Chembiochem – volume: 123 start-page: 6098 year: 2001 end-page: 6107 ident: bb0410 article-title: Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins publication-title: J. Am. Chem. Soc. – volume: 467 start-page: 868 year: 2010 end-page: 871 ident: bb1140 article-title: The proteasome antechamber maintains substrates in an unfolded state publication-title: Nature – volume: 13 start-page: 375 year: 1999 end-page: 380 ident: bb0540 article-title: Efficient determination of angles subtended by Ca-Ha and N-HN vectors in proteins via dipole-dipole cross-correlation publication-title: J. Biomol. NMR – volume: 54 start-page: 6983 year: 2015 end-page: 6995 ident: bb0870 article-title: Differential large-amplitude breathing motions in the interface of FKBP12-drug complexes publication-title: Biochemistry – volume: 97 start-page: 495 year: 1979 end-page: 502 ident: bb1370 article-title: Polymerization of the bacterial elongation factor for protein synthesis, EF-Tu publication-title: Eur. J. Biochem. – volume: 122 start-page: 5105 year: 2000 end-page: 5113 ident: bb0525 article-title: Ubiquitin backbone motion studied via NH N publication-title: J. Am. Chem. Soc. – volume: 24 start-page: 1714 year: 2015 end-page: 1719 ident: bb0640 article-title: Population shuffling between ground and high energy excited states publication-title: Protein Sci. – volume: 31 start-page: 5253 year: 1992 end-page: 5263 ident: bb0295 article-title: Dynamics of methyl groups in proteins as studied by proton-detected 13CNMR spectroscopy. Application to the leucine residues of staphylococcal nuclease? publication-title: Biochemistry – volume: 13 start-page: 570 year: 2003 end-page: 580 ident: bb0890 article-title: TROSY in NMR studies of the structure and function of large biological macromolecules publication-title: Curr. Opin. Struct. Biol. – volume: 127 start-page: 8014 year: 2005 end-page: 8015 ident: bb0780 article-title: Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds publication-title: J. Am. Chem. Soc. – volume: 132 start-page: 9392 year: 2010 end-page: 9397 ident: bb1270 article-title: Effects of proteins on protein diffusion publication-title: J. Am. Chem. Soc. – volume: 134 start-page: 12817 year: 2012 end-page: 12829 ident: bb1330 article-title: A new algorithm for reliable and general NMR resonance assignment publication-title: J. Am. Chem. Soc. – volume: 17 start-page: 1169 year: 2009 end-page: 1185 ident: bb0505 article-title: Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings publication-title: Struct. Fold. Des. – volume: 328 start-page: 98 year: 2010 end-page: 102 ident: bb1135 article-title: Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR publication-title: Science – volume: 129 start-page: 4724 year: 2007 end-page: 4730 ident: bb0490 article-title: Exploring multiple timescale motions in protein GB3 using accelerated molecular dynamics and NMR spectroscopy publication-title: J. Am. Chem. Soc. – volume: 188 start-page: 295 year: 2007 end-page: 300 ident: bb0980 article-title: NMR data processing using iterative thresholding and minimum l(1)-norm reconstruction publication-title: J. Magn. Reson. – volume: 114 start-page: 6661 year: 2014 end-page: 6714 ident: bb0255 article-title: Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs) publication-title: Chem. Rev. – volume: 9 start-page: 462 year: 2013 end-page: 465 ident: bb0085 article-title: Allosteric inhibition through suppression of transient conformational states publication-title: Nat. Chem. Biol. – volume: 104 start-page: 18473 year: 2007 end-page: 18477 ident: bb0690 article-title: Measurement of bond vector orientations in invisible excited states of proteins publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 109 start-page: 4108 year: 2009 end-page: 4139 ident: bb1035 article-title: Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes publication-title: Chem. Rev. – volume: 128 start-page: 951 year: 2006 end-page: 956 ident: bb0760 article-title: Real-time monitoring of chemical transformations by ultrafast 2D NMR spectroscopy publication-title: J. Am. Chem. Soc. – volume: 109 start-page: 21216 year: 2012 end-page: 21222 ident: bb0495 article-title: Allosteric networks in thrombin distinguish procoagulant vs. anticoagulant activities publication-title: Proc. Natl. Acad. Sci. – volume: 430 start-page: 586 year: 2004 end-page: 590 ident: bb0685 article-title: Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR publication-title: Nature – volume: 6 start-page: 38312 year: 2016 ident: bb1340 article-title: Improved in-cell structure determination of proteins at near-physiological concentration publication-title: Sci Rep – volume: 128 start-page: 13421 year: 2006 end-page: 13426 ident: bb0940 article-title: Targeted acquisition for real-time NMR spectroscopy publication-title: J. Am. Chem. Soc. – volume: 480 start-page: 268 year: 2011 end-page: 272 ident: bb0715 article-title: Atomic-resolution dynamics on the surface of amyloid-b protofibrils probed by solution NMR publication-title: Nature – volume: 110 start-page: 12867 year: 2013 end-page: 12874 ident: bb0030 article-title: NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 27 start-page: 157 year: 2009 end-page: 167 ident: bb0025 article-title: Protein promiscuity and its implications for biotechnology publication-title: Nat. Biotechnol. – volume: 6 start-page: 1536 year: 2005 end-page: 1549 ident: bb1010 article-title: NMR spectroscopy of paramagnetic metalloproteins publication-title: Chembiochem – volume: 37 start-page: 375 year: 2008 end-page: 397 ident: bb1275 article-title: Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences publication-title: Annu. Rev. Biophys. – volume: 2 start-page: 527 year: 2003 end-page: 541 ident: bb0090 article-title: Implications of protein flexibility for drug discovery publication-title: Nat. Rev. Drug Discov. – volume: 25 start-page: 265 year: 2003 end-page: 280 ident: bb0515 article-title: Correlated motions of successive amide N publication-title: J. Biomol. NMR – volume: 143 start-page: 45 year: 2000 end-page: 68 ident: bb0135 article-title: Cross-correlated relaxation for the measurement of angles between Tensorial interactions publication-title: J. Magn. Reson. – start-page: 1 year: 2015 end-page: 33 ident: bb0100 article-title: Thermal Fluctuations of Immature SOD1 Lead to Separate Folding and Misfolding Pathways – volume: 131 start-page: 15761 year: 2009 end-page: 15768 ident: bb1230 article-title: Evaluation of parameters critical for observing nucleic acids inside living publication-title: J. Am. Chem. Soc. – volume: 17 start-page: 195 year: 2000 end-page: 202 ident: bb0885 article-title: [N-15,H-1]/[C-13,H-1]-TROSY for simultaneous detection of backbone N-15-H-1, aromatic C-13-H-1 and side-chain N-15-H-1(2) correlations in large proteins publication-title: J. Biomol. NMR – volume: 133 start-page: 13790 year: 2011 end-page: 13793 ident: bb0570 article-title: NMR cross-correlated relaxation rates reveal ion coordination sites in DNA publication-title: J. Am. Chem. Soc. – volume: 182 start-page: 96 year: 2006 end-page: 105 ident: bb0900 article-title: Spectral reconstruction methods in fast NMR: reduced dimensionality, random sampling and maximum entropy publication-title: J. Magn. Reson. – volume: 133 start-page: 11154 year: 2011 end-page: 11162 ident: bb0740 article-title: Transient enzyme–substrate recognition monitored by real-time NMR publication-title: J. Am. Chem. Soc. – volume: 38 start-page: 129 year: 2009 end-page: 143 ident: bb1110 article-title: Automated structure determination from NMR spectra publication-title: Eur. Biophys. J. – volume: 103 start-page: 11904 year: 2006 end-page: 11909 ident: bb1175 article-title: Quantitative NMR analysis of the protein G B1 domain in publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 102 start-page: 18908 year: 2005 end-page: 18913 ident: bb0020 article-title: Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state publication-title: Proc. Natl. Acad. Sci. – volume: 7 year: 2007 ident: bb0070 article-title: Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: a case study of antibodies publication-title: BMC Struct. Biol. – volume: 102 start-page: 622 year: 2005 end-page: 627 ident: bb1065 article-title: Solution NMR-derived global fold of a monomeric 82-kDa enzyme publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 9 start-page: 504 year: 2010 end-page: 510 ident: bb0770 article-title: In situ NMR observation of the formation of metallic lithium microstructures in lithium batteries publication-title: Nat. Mater. – volume: 30 start-page: 129 year: 2003 end-page: 155 ident: bb0125 article-title: NMR probes of molecular dynamics: overview and comparison with other techniques publication-title: Annu. Rev. Biophys. Biomol. Struct. – volume: 50 start-page: 5556 year: 2011 end-page: 5559 ident: bb0970 article-title: Accelerated NMR spectroscopy by using compressed sensing publication-title: Angew. Chem. Int. Ed. Eng. – volume: 269 start-page: 65 year: 2016 end-page: 69 ident: bb0730 article-title: High-power 1H composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments publication-title: J. Magn. Reson. – volume: 34 start-page: 6784 year: 1995 end-page: 6794 ident: bb1285 article-title: Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer publication-title: Biochemistry – volume: 47 start-page: 5235 year: 2008 end-page: 5237 ident: bb0785 article-title: Time-resolved dynamic nuclear polarization enhanced NMR spectroscopy publication-title: Angew. Chem. Int. Ed. – volume: 58 start-page: 129 year: 2014 end-page: 139 ident: bb0950 article-title: Time-resolved multidimensional NMR with non-uniform sampling publication-title: J. Biomol. NMR – volume: 133 start-page: 9063 year: 2011 end-page: 9068 ident: bb1145 article-title: Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease publication-title: J. Am. Chem. Soc. – volume: 13 start-page: 527 year: 2010 end-page: 537 ident: bb0095 article-title: Conformational ensembles, signal transduction and residue hot spots: application to drug discovery publication-title: Curr. Opin. Drug Discov. Devel. – volume: 24 start-page: 706 year: 2015 end-page: 713 ident: bb1300 article-title: Hydrogen exchange of disordered proteins in publication-title: Protein Sci. – volume: 121 start-page: 6876 year: 1999 end-page: 6883 ident: bb0535 article-title: Relaxation of two-spin coherence due to cross-correlated fluctuations of dipole publication-title: J. Am. Chem. Soc. – volume: 41 start-page: 214 year: 2008 end-page: 221 ident: bb0045 article-title: Characterization of enzyme motions by solution NMR relaxation dispersion publication-title: Acc. Chem. Res. – volume: 40 start-page: 95 year: 2008 end-page: 106 ident: bb1055 article-title: Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints publication-title: J. Biomol. NMR – volume: 115 start-page: 13740 year: 2011 end-page: 13745 ident: bb0960 article-title: Boosting protein dynamics studies using quantitative nonuniform sampling NMR spectroscopy publication-title: J. Phys. Chem. B – volume: 120 start-page: 10571 year: 1998 end-page: 10572 ident: bb1020 article-title: Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses publication-title: J. Am. Chem. Soc. – volume: 178 start-page: 72 year: 2006 end-page: 76 ident: bb0225 article-title: Effective rotational correlation times of proteins from NMR relaxation interference publication-title: J. Magn. Reson. – volume: 120 start-page: 11919 year: 2004 end-page: 11929 ident: bb0480 article-title: Accelerated molecular dynamics: a promising and efficient simulation method for biomolecules publication-title: J. Chem. Phys. – volume: 3 start-page: 605 year: 2006 end-page: 607 ident: bb0945 article-title: Removal of a time barrier for high-resolution multidimensional NMR spectroscopy publication-title: Nat. Methods – volume: 119 start-page: 6672 year: 1997 end-page: 6673 ident: bb0430 article-title: Locally anisotropic internal polypeptide backbone dynamics by NMR relaxation publication-title: J. Am. Chem. Soc. – volume: 129 year: 2007 ident: bb0835 article-title: A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues publication-title: J. Am. Chem. Soc. – volume: 112 start-page: 12402 year: 2015 end-page: 12407 ident: bb1225 article-title: Thermodynamics of protein destabilization in live cells publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 109 start-page: 988 year: 2015 end-page: 999 ident: bb0260 article-title: Distribution of Pico- and Nanosecond motions in disordered proteins from nuclear spin relaxation publication-title: Biophys. J. – volume: 18 start-page: 1401 year: 2009 end-page: 1424 ident: bb0285 article-title: Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain publication-title: Protein Sci. – volume: 113 start-page: 3269 year: 2016 end-page: 3274 ident: bb0645 article-title: Allosteric switch regulates protein–protein binding through collective motion publication-title: Proc. Natl. Acad. Sci. – volume: 7 start-page: 549 year: 2011 ident: bb1375 article-title: The quantitative proteome of a human cell line publication-title: Mol. Syst. Biol. – volume: 115 start-page: 9832 year: 1993 end-page: 9833 ident: bb0320 article-title: NMR order parameters and free energy: an analytical approach and its application to cooperative Ca2 publication-title: J. Am. Chem. Soc. – volume: 120 start-page: 8313 year: 2016 end-page: 8320 ident: bb0335 article-title: Picosecond to millisecond structural dynamics in human ubiquitin publication-title: J. Phys. Chem. B – volume: 132 start-page: 10992 year: 2010 end-page: 10995 ident: bb0660 article-title: 13CHD 2Methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics publication-title: J. Am. Chem. Soc. – volume: 14 start-page: 277 year: 1999 end-page: 280 ident: bb0545 article-title: Simultaneous determination of psi and phi angles in proteins from measurements of cross-correlated relaxation effects publication-title: J. Biomol. NMR – volume: 83 start-page: 1177 year: 2002 end-page: 1183 ident: bb1040 article-title: Quaternary structure built from subunits combining NMR and small-angle X-ray scattering data publication-title: Biophys. J. – volume: 109 start-page: E3454 year: 2012 end-page: E3462 ident: bb1150 article-title: Proteasome allostery as a population shift between interchanging conformers publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 111 start-page: 5532 year: 2014 end-page: 5537 ident: bb1160 article-title: Understanding the mechanism of proteasome 20S core particle gating publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 66 start-page: 99 year: 2016 end-page: 110 ident: bb1355 article-title: A new carbamidemethyl-linked lanthanoid chelating tag for PCS NMR spectroscopy of proteins in living HeLa cells publication-title: J. Biomol. NMR – volume: 129 start-page: 1743 year: 2007 end-page: 1750 ident: bb1130 article-title: Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy publication-title: J. Am. Chem. Soc. – volume: 41 start-page: 442 year: 2008 end-page: 451 ident: bb0610 article-title: Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding publication-title: Acc. Chem. Res. – volume: 131 start-page: 10834 year: 2009 end-page: 10835 ident: bb1220 article-title: Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin o publication-title: J. Am. Chem. Soc. – volume: 12 start-page: 713 year: 1999 end-page: 720 ident: bb0465 article-title: Folding funnels and binding mechanisms publication-title: Protein Eng. – volume: 32 start-page: 281 year: 2005 end-page: 293 ident: bb0635 article-title: A new amide proton R1rho experiment permits accurate characterization of microsecond time-scale conformational exchange publication-title: J. Biomol. NMR – volume: 73 start-page: 69 year: 1987 end-page: 77 ident: bb0905 article-title: Exponential sampling, an alternative method for sampling in two-dimensional Nmr experiments publication-title: J. Magn. Reson. – year: 2013 ident: bb1200 article-title: In-cell NMR Spectroscopy in Mammalian Cells – volume: 122 start-page: 1758 year: 2000 end-page: 1761 ident: bb0530 article-title: Relative orientation of C αH α-bond vectors of successive residues in proteins through cross-correlated relaxation in NMR publication-title: J. Am. Chem. Soc. – volume: 329 start-page: 1312 year: 2010 end-page: 1316 ident: bb0650 article-title: A transient and low-populated protein-folding intermediate at atomic resolution publication-title: Science – volume: 129 start-page: 13396 year: 2007 end-page: 13397 ident: bb0695 article-title: Characterization of chemical exchange using residual dipolar coupling publication-title: J. Am. Chem. Soc. – volume: 62 start-page: 373 year: 2015 end-page: 385 ident: bb0795 article-title: An economic approach to efficient isotope labeling in insect cells using homemade 15N-, 13C- and 2H-labeled yeast extracts publication-title: J. Biomol. NMR – volume: 268 start-page: 886 year: 1995 end-page: 891 ident: bb0245 article-title: Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling publication-title: Science – volume: 54 start-page: 5328 year: 2015 end-page: 5330 ident: bb1350 article-title: Direct observation of Ca(2 publication-title: Angew. Chem. Int. Ed. Eng. – year: 2015 ident: bb0675 article-title: Characterizing RNA Excited States Using NMR Relaxation Dispersion – volume: 102 start-page: 13885 year: 2005 end-page: 13890 ident: bb0435 article-title: Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings publication-title: Proc. Natl. Acad. Sci. – volume: 2 start-page: 865 year: 1995 end-page: 870 ident: bb0755 article-title: Following protein folding in real time using NMR spectroscopy publication-title: Nat. Struct. Biol. – volume: 116 start-page: 8426 year: 1994 end-page: 8427 ident: bb0425 article-title: NMR order parameters of biomolecules: a new analytical representation and application to the Gaussian axial fluctuation model publication-title: J. Am. Chem. Soc. – volume: 58 start-page: 287 year: 2014 end-page: 301 ident: bb0420 article-title: ORIUM: optimized RDC-based iterative and unified model-free analysis publication-title: J. Biomol. NMR – volume: 4 start-page: 849 year: 1997 end-page: 853 ident: bb0015 article-title: NMR structures of proteins and protein complexes beyond 20,000 M-r publication-title: Nat. Struct. Biol. – volume: 108 start-page: 9839 year: 2011 end-page: 9844 ident: bb0355 article-title: Intrinsic disorder in measles virus nucleocapsids publication-title: Proc. Natl. Acad. Sci. – volume: 133 start-page: 10336 year: 2011 end-page: 10339 ident: bb0590 article-title: Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition publication-title: J. Am. Chem. Soc. – volume: 445 start-page: 618 year: 2007 end-page: 622 ident: bb1125 article-title: Quantitative dynamics and binding studies of the 20S proteasome by NMR publication-title: Nature – volume: 98 start-page: 3185 year: 2001 end-page: 3190 ident: bb1250 article-title: Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O publication-title: Proc. Natl. Acad. Sci. – volume: 135 start-page: 5457 year: 2013 end-page: 5466 ident: bb0455 article-title: A general method for constructing atomic-resolution RNA ensembles using NMR residual dipolar couplings: the basis for interhelical motions revealed publication-title: J. Am. Chem. Soc. – volume: 129 start-page: 5108 year: 2007 end-page: 5116 ident: bb0930 article-title: Ultrahigh-resolution H-1-C-13 HSQC spectra of metabolite mixtures using nonlinear sampling and forward maximum entropy reconstruction publication-title: J. Am. Chem. Soc. – volume: 135 start-page: 9259 year: 2013 end-page: 9262 ident: bb1155 article-title: Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR publication-title: J. Am. Chem. Soc. – volume: 134 start-page: 12798 year: 2012 end-page: 12806 ident: bb1170 article-title: Structure of proteins in eukaryotic compartments publication-title: J. Am. Chem. Soc. – volume: 48 start-page: 35 year: 2015 end-page: 116 ident: bb0700 article-title: Visualizing transient dark states by NMR spectroscopy publication-title: Q. Rev. Biophys. – volume: 57 start-page: 73 year: 2013 end-page: 82 ident: bb0735 article-title: Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy publication-title: J. Biomol. NMR – volume: 119 start-page: 7599 year: 1997 end-page: 7600 ident: bb0815 article-title: Production and incorporation of N-15, C-13, H-2 (H-1-delta 1 methyl) isoleucine into proteins for multidimensional NMR studies publication-title: J. Am. Chem. Soc. – volume: 52 start-page: 11410 year: 2013 end-page: 11414 ident: bb0240 article-title: Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes publication-title: Angew. Chem. Int. Ed. – volume: 28 start-page: 8972 year: 1989 end-page: 8979 ident: bb0150 article-title: Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease publication-title: Biochemistry – volume: 127 start-page: 16621 year: 2005 end-page: 16628 ident: bb1045 article-title: Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data publication-title: J. Am. Chem. Soc. – volume: 128 start-page: 13421 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0940 article-title: Targeted acquisition for real-time NMR spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja062146p – volume: 202 start-page: 140 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb1380 article-title: A bioreactor for in-cell protein NMR publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2009.10.008 – volume: 108 start-page: 9839 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0355 article-title: Intrinsic disorder in measles virus nucleocapsids publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1103270108 – volume: 120 start-page: 11919 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb0480 article-title: Accelerated molecular dynamics: a promising and efficient simulation method for biomolecules publication-title: J. Chem. Phys. doi: 10.1063/1.1755656 – volume: 8 start-page: 610 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0840 article-title: Synthesis of a13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy publication-title: Chembiochem doi: 10.1002/cbic.200600551 – volume: 207 start-page: 294 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0205 article-title: On the measurement of 15N-{1H} nuclear Overhauser effects. 2. Effects of the saturation scheme and water signal suppression publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2010.09.014 – volume: 295 start-page: 1719 year: 2002 ident: 10.1016/j.bbagen.2017.08.020_bb0280 article-title: Long-range interactions within a nonnative protein publication-title: Science doi: 10.1126/science.1067680 – volume: 182 start-page: 96 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0900 article-title: Spectral reconstruction methods in fast NMR: reduced dimensionality, random sampling and maximum entropy publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2006.06.007 – volume: 52 start-page: 3911 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0235 article-title: Internal dynamics of the homotrimeric HIV-1 viral coat protein gp41 on multiple time scales publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.201207266 – volume: 64 start-page: 165 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0965 article-title: Non-uniform sampling of NMR relaxation data publication-title: J. Biomol. NMR doi: 10.1007/s10858-016-0020-6 – volume: 102 start-page: 6679 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb0115 article-title: Molecular dynamics and protein function publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0408930102 – volume: 104 start-page: 4559 year: 1982 ident: 10.1016/j.bbagen.2017.08.020_bb0155 article-title: Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00381a010 – volume: 269 start-page: 65 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0730 article-title: High-power 1H composite pulse decoupling provides artifact free exchange-mediated saturation transfer (EST) experiments publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2016.05.013 – volume: 57 start-page: 73 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0735 article-title: Enhanced accuracy of kinetic information from CT-CPMG experiments by transverse rotating-frame spectroscopy publication-title: J. Biomol. NMR doi: 10.1007/s10858-013-9769-z – volume: 127 start-page: 184 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0185 – volume: 50 start-page: 137 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb1325 article-title: Exclusively NOESY-based automated NMR assignment and structure determination of proteins publication-title: J. Biomol. NMR doi: 10.1007/s10858-011-9502-8 – volume: 34 start-page: 6784 year: 1995 ident: 10.1016/j.bbagen.2017.08.020_bb1285 article-title: Structural characterization of folded and unfolded states of an SH3 domain in equilibrium in aqueous buffer publication-title: Biochemistry doi: 10.1021/bi00020a025 – volume: 104 start-page: 6644 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb1025 article-title: DNA-nanotube-induced alignment of membrane proteins for NMR structure determination publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0700930104 – volume: 2 start-page: 527 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb0090 article-title: Implications of protein flexibility for drug discovery publication-title: Nat. Rev. Drug Discov. doi: 10.1038/nrd1129 – volume: 15 start-page: 241 year: 1999 ident: 10.1016/j.bbagen.2017.08.020_bb0555 article-title: Determination of sugar conformation in large RNA oligonucleotides from analysis of dipole–dipole cross correlated relaxation by solution NMR spectroscopy publication-title: J. Biomol. NMR doi: 10.1023/A:1008319130714 – volume: 50 start-page: 11437 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0630 article-title: Kinetics of conformational sampling in ubiquitin publication-title: Angew. Chem. Int. Ed. Eng. doi: 10.1002/anie.201105086 – volume: 16 start-page: 746 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0855 article-title: Novel approaches in selective tryptophan isotope labeling by using Escherichia coli overexpression media publication-title: Chembiochem doi: 10.1002/cbic.201402677 – year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1200 – volume: 430 start-page: 586 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb0685 article-title: Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR publication-title: Nature doi: 10.1038/nature02655 – volume: 188 start-page: 295 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0980 article-title: NMR data processing using iterative thresholding and minimum l(1)-norm reconstruction publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2007.07.008 – volume: 13 start-page: 28 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0010 article-title: How good can cryo-EM become? publication-title: Nat. Methods doi: 10.1038/nmeth.3695 – volume: 9 start-page: 504 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0770 article-title: In situ NMR observation of the formation of metallic lithium microstructures in lithium batteries publication-title: Nat. Mater. doi: 10.1038/nmat2764 – volume: 126 start-page: 9827 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb1070 article-title: Stereospecific NMR assignments of prochiral methyls, rotameric states and dynamics of valine residues in malate synthase G publication-title: J. Am. Chem. Soc. doi: 10.1021/ja048738u – volume: 25 start-page: 265 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb0515 article-title: Correlated motions of successive amide NH bonds in proteins publication-title: J. Biomol. NMR doi: 10.1023/A:1023076212536 – volume: 132 start-page: 9392 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb1270 article-title: Effects of proteins on protein diffusion publication-title: J. Am. Chem. Soc. doi: 10.1021/ja102296k – volume: 105 start-page: 4685 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb1360 article-title: Consistent blind protein structure generation from NMR chemical shift data publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0800256105 – volume: 54 start-page: 6983 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0870 article-title: Differential large-amplitude breathing motions in the interface of FKBP12-drug complexes publication-title: Biochemistry doi: 10.1021/acs.biochem.5b00820 – volume: 38 start-page: 197 year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb0145 article-title: NMR studies of Brownian tumbling and internal motions in proteins publication-title: Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/S0079-6565(00)00028-5 – volume: 34 start-page: 129 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0625 article-title: Assessment of the effects of increased relaxation dispersion data on the extraction of 3-site exchange parameters characterizing the unfolding of an SH3 domain publication-title: J. Biomol. NMR doi: 10.1007/s10858-006-0001-2 – volume: 102 start-page: 622 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb0400 – volume: 13 start-page: 570 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb0890 article-title: TROSY in NMR studies of the structure and function of large biological macromolecules publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2003.09.009 – volume: 129 start-page: 11468 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0170 article-title: An exchange-free measure of 15N transverse relaxation: an NMR spectroscopy application to the study of a folding intermediate with pervasive chemical exchange publication-title: J. Am. Chem. Soc. doi: 10.1021/ja072717t – volume: 53 start-page: 209 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0190 article-title: Measurement of 15N relaxation rates in perdeuterated proteins by TROSY-based methods publication-title: J. Biomol. NMR doi: 10.1007/s10858-012-9626-5 – volume: 438 start-page: 653 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1245 article-title: An in-cell NMR study of monitoring stress-induced increase of cytosolic Ca2+ concentration in HeLa cells publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2013.07.127 – volume: 114 start-page: 6661 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0255 article-title: Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs) publication-title: Chem. Rev. doi: 10.1021/cr400695p – volume: 133 start-page: 9063 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb1145 article-title: Site-directed methyl group labeling as an NMR probe of structure and dynamics in supramolecular protein systems: applications to the proteasome and to the ClpP protease publication-title: J. Am. Chem. Soc. doi: 10.1021/ja202259a – volume: 36 start-page: 179 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb1180 article-title: In-cell NMR spectroscopy of proteins inside Xenopus laevis oocytes publication-title: J. Biomol. NMR doi: 10.1007/s10858-006-9079-9 – volume: 462 start-page: 151 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb1210 – volume: 66 start-page: 99 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1355 article-title: A new carbamidemethyl-linked lanthanoid chelating tag for PCS NMR spectroscopy of proteins in living HeLa cells publication-title: J. Biomol. NMR doi: 10.1007/s10858-016-0059-4 – volume: 254 start-page: 1598 year: 1991 ident: 10.1016/j.bbagen.2017.08.020_bb0060 article-title: The energy landscapes and motions of proteins publication-title: Science doi: 10.1126/science.1749933 – volume: 182 start-page: 167 year: 1993 ident: 10.1016/j.bbagen.2017.08.020_bb1255 article-title: A guide to the use of pore-forming toxins for controlled permeabilization of cell membranes publication-title: Med. Microbiol. Immunol. doi: 10.1007/BF00219946 – volume: 339 start-page: 1080 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1085 article-title: Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction publication-title: Science doi: 10.1126/science.1233066 – volume: 122 start-page: 6779 year: 2000 ident: 10.1016/j.bbagen.2017.08.020_bb0580 article-title: NMR determination of sugar puckers in nucleic Acids from CSA−dipolar cross-correlated relaxation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja000976b – volume: 7 start-page: 549 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb1375 article-title: The quantitative proteome of a human cell line publication-title: Mol. Syst. Biol. doi: 10.1038/msb.2011.82 – volume: 31 start-page: 5253 year: 1992 ident: 10.1016/j.bbagen.2017.08.020_bb0295 article-title: Dynamics of methyl groups in proteins as studied by proton-detected 13CNMR spectroscopy. Application to the leucine residues of staphylococcal nuclease? publication-title: Biochemistry doi: 10.1021/bi00138a003 – volume: 121 start-page: 1945 year: 1999 ident: 10.1016/j.bbagen.2017.08.020_bb0585 article-title: Transferred cross-correlated relaxation: application to the determination of sugar pucker in an Aminoacylated tRNA-mimetic weakly bound to EF-Tu publication-title: J. Am. Chem. Soc. doi: 10.1021/ja9835887 – volume: 28 start-page: 205 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb1015 article-title: Improving the accuracy of NMR structures of large proteins using pseudocontact shifts as long-range restraints publication-title: J. Biomol. NMR doi: 10.1023/B:JNMR.0000013706.09264.36 – volume: 52 start-page: 10237 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1240 article-title: 3D structure determination of a protein in living cells using paramagnetic NMR spectroscopy publication-title: Chem. Commun. (Camb.) doi: 10.1039/C6CC05490K – volume: 48 start-page: 8023 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0500 article-title: Functional dynamics of the folded Ankyrin repeats of IκBα revealed by nuclear magnetic resonance publication-title: Biochemistry doi: 10.1021/bi900712r – volume: 127 start-page: 8014 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb0780 article-title: Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds publication-title: J. Am. Chem. Soc. doi: 10.1021/ja051306e – volume: 121 start-page: 6876 year: 1999 ident: 10.1016/j.bbagen.2017.08.020_bb0535 article-title: Relaxation of two-spin coherence due to cross-correlated fluctuations of dipole−dipole couplings and anisotropic shifts in NMR of 15N, 13C-labeled biomolecules publication-title: J. Am. Chem. Soc. doi: 10.1021/ja984390p – year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0675 – volume: 326 start-page: 47 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb1030 article-title: The use of residual dipolar coupling in studying proteins by NMR publication-title: Top. Curr. Chem. doi: 10.1007/128_2011_215 – volume: 126 start-page: 1962 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb0565 article-title: Determination of the glycosidic bond angle chi in RNA from cross-correlated relaxation of CH dipolar coupling and N chemical shift anisotropy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0367041 – volume: 51 start-page: 57 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0615 article-title: The feasibility of parameterizing four-state equilibria using relaxation dispersion measurements publication-title: J. Biomol. NMR doi: 10.1007/s10858-011-9541-1 – volume: 94 start-page: 12366 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0220 article-title: Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.94.23.12366 – volume: 32 start-page: 281 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb0635 article-title: A new amide proton R1rho experiment permits accurate characterization of microsecond time-scale conformational exchange publication-title: J. Biomol. NMR doi: 10.1007/s10858-005-0658-y – volume: 221 start-page: 1 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0600 article-title: Exceeding the limit of dynamics studies on biomolecules using high spin-lock field strengths with a cryogenically cooled probehead publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2012.05.005 – volume: 50 start-page: 5556 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0970 article-title: Accelerated NMR spectroscopy by using compressed sensing publication-title: Angew. Chem. Int. Ed. Eng. doi: 10.1002/anie.201100370 – volume: 34 start-page: 65 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb0745 article-title: Protein folding studied by real-time NMR spectroscopy publication-title: Methods doi: 10.1016/j.ymeth.2004.03.014 – volume: 7 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0830 article-title: An economical method for production of (2)H, (13)CH3-threonine for solution NMR studies of large protein complexes: application to the 670kDa proteasome publication-title: PLoS One doi: 10.1371/journal.pone.0043725 – volume: 56 start-page: 346 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0800 article-title: Stable-isotope-assisted NMR approaches to glycoproteins using immunoglobulin G as a model system publication-title: Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/j.pnmrs.2010.03.001 – volume: 59 start-page: 360 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb1215 article-title: Expanding the utility of NMR restraints with paramagnetic compounds: background and practical aspects publication-title: Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/j.pnmrs.2011.05.001 – volume: 109 start-page: 988 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0260 article-title: Distribution of Pico- and Nanosecond motions in disordered proteins from nuclear spin relaxation publication-title: Biophys. J. doi: 10.1016/j.bpj.2015.06.069 – volume: 18 start-page: 1401 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0285 article-title: Paramagnetic relaxation enhancements in unfolded proteins: theory and application to drkN SH3 domain publication-title: Protein Sci. doi: 10.1002/pro.153 – volume: 57 start-page: 111 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0140 article-title: Nuclear spin relaxation in isotropic and anisotropic media publication-title: Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/j.pnmrs.2010.04.003 – volume: 129 start-page: 4724 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0490 article-title: Exploring multiple timescale motions in protein GB3 using accelerated molecular dynamics and NMR spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0687668 – volume: 17 start-page: 195 year: 2000 ident: 10.1016/j.bbagen.2017.08.020_bb0885 article-title: [N-15,H-1]/[C-13,H-1]-TROSY for simultaneous detection of backbone N-15-H-1, aromatic C-13-H-1 and side-chain N-15-H-1(2) correlations in large proteins publication-title: J. Biomol. NMR doi: 10.1023/A:1008399320576 – volume: 135 start-page: 1688 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0935 article-title: High-resolution heteronuclear multidimensional NMR of proteins in living insect cells using a baculovirus protein expression system publication-title: J. Am. Chem. Soc. doi: 10.1021/ja310928u – volume: 9 start-page: 1024 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb1185 article-title: Interaction of alpha-synuclein and a cell penetrating fusion peptide with higher eukaryotic cell membranes assessed by (1)(9)F NMR publication-title: Mol. Pharm. doi: 10.1021/mp200615m – volume: 21 start-page: 883 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1365 article-title: Three-dimensional protein fold determination from backbone amide pseudocontact shifts generated by lanthanide tags at multiple sites publication-title: Structure doi: 10.1016/j.str.2013.04.001 – volume: 125 start-page: 10420 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb0895 article-title: Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes publication-title: J. Am. Chem. Soc. doi: 10.1021/ja030153x – volume: 23 start-page: 172 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0365 article-title: Chemical shifts in biomolecules publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2013.01.007 – volume: 106 start-page: 13737 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0460 article-title: Conformational selection or induced fit: a flux description of reaction mechanism publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0907195106 – volume: 27 start-page: 81 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb0845 article-title: A novel method for the biosynthesis of deuterated proteins with selective protonation at the aromatic rings of Phe, Tyr and Trp publication-title: J. Biomol. NMR doi: 10.1023/A:1024710729352 – volume: 37 start-page: 375 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb1275 article-title: Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences publication-title: Annu. Rev. Biophys. doi: 10.1146/annurev.biophys.37.032807.125817 – volume: 537 start-page: 202 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1100 article-title: Structural basis for the antifolding activity of a molecular chaperone publication-title: Nature doi: 10.1038/nature18965 – volume: 458 start-page: 102 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb1315 article-title: Protein structure determination in living cells by in-cell NMR spectroscopy publication-title: Nature doi: 10.1038/nature07814 – volume: 299 start-page: 1362 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb0080 article-title: Antibody multispecificity mediated by conformational diversity publication-title: Science doi: 10.1126/science.1079731 – volume: 21 start-page: 1102 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0035 article-title: Small-molecule inhibitors of protein-protein interactions: progressing toward the reality publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2014.09.001 – volume: 49 start-page: 6984 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb1265 article-title: Volume exclusion and soft interaction effects on protein stability under crowded conditions publication-title: Biochemistry doi: 10.1021/bi100727y – volume: 329 start-page: 1312 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0650 article-title: A transient and low-populated protein-folding intermediate at atomic resolution publication-title: Science doi: 10.1126/science.1191723 – volume: 106 start-page: 1700 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0655 article-title: Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy publication-title: Chem. Rev. doi: 10.1021/cr0404287 – volume: 122 start-page: 1758 year: 2000 ident: 10.1016/j.bbagen.2017.08.020_bb0530 article-title: Relative orientation of C αH α-bond vectors of successive residues in proteins through cross-correlated relaxation in NMR publication-title: J. Am. Chem. Soc. doi: 10.1021/ja9933184 – volume: 35 start-page: 16843 year: 1996 ident: 10.1016/j.bbagen.2017.08.020_bb0750 article-title: Real-time refolding studies of 6-19F-tryptophan labeled Escherichia Coli dihydrofolate reductase using stopped-flow NMR spectroscopy publication-title: Biochemistry doi: 10.1021/bi961896g – volume: 109 start-page: 21216 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0495 article-title: Allosteric networks in thrombin distinguish procoagulant vs. anticoagulant activities publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1218414109 – start-page: 194 year: 2017 ident: 10.1016/j.bbagen.2017.08.020_bb0805 article-title: Stable isotope labeling of glycoproteins for NMR study – volume: 154 start-page: 157 year: 2002 ident: 10.1016/j.bbagen.2017.08.020_bb0620 article-title: R1ρ relaxation outside of the fast-exchange limit publication-title: J. Magn. Reson. doi: 10.1006/jmre.2001.2466 – volume: 117 start-page: 11536 year: 1995 ident: 10.1016/j.bbagen.2017.08.020_bb0300 article-title: Measurement of 2H T1 and T1rho relaxation times in uniformly 13C-labeled and fractionally 2H-labeled proteins in solution publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00151a018 – volume: 263 start-page: 627 year: 1996 ident: 10.1016/j.bbagen.2017.08.020_bb0810 article-title: Selective methyl group protonation of perdeuterated proteins publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1996.0603 – volume: 111 start-page: 5532 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb1160 article-title: Understanding the mechanism of proteasome 20S core particle gating publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1322079111 – volume: 458 start-page: 106 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb1195 article-title: High-resolution multi-dimensional NMR spectroscopy of proteins in human cells publication-title: Nature doi: 10.1038/nature07839 – volume: 17 start-page: 1169 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0505 article-title: Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings publication-title: Struct. Fold. Des. doi: 10.1016/j.str.2009.08.001 – volume: 344 start-page: 1250494 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb1120 article-title: Structural basis for protein antiaggregation activity of the trigger factor chaperone publication-title: Science doi: 10.1126/science.1250494 – volume: 112 start-page: 12402 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb1225 article-title: Thermodynamics of protein destabilization in live cells publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1511308112 – volume: 50 start-page: 10189 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0820 article-title: Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes publication-title: Biochemistry doi: 10.1021/bi201496d – volume: 131 start-page: 15761 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb1230 article-title: Evaluation of parameters critical for observing nucleic acids inside living Xenopus laevis oocytes by in-cell NMR spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja9052027 – volume: 112 start-page: 4989 year: 1990 ident: 10.1016/j.bbagen.2017.08.020_bb0175 article-title: Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00168a070 – volume: 386 start-page: 391 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0665 article-title: Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2008.11.055 – volume: 115 start-page: 13740 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0960 article-title: Boosting protein dynamics studies using quantitative nonuniform sampling NMR spectroscopy publication-title: J. Phys. Chem. B doi: 10.1021/jp2081116 – volume: 135 start-page: 9259 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1155 article-title: Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR publication-title: J. Am. Chem. Soc. doi: 10.1021/ja403091c – volume: 3 start-page: 605 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0945 article-title: Removal of a time barrier for high-resolution multidimensional NMR spectroscopy publication-title: Nat. Methods doi: 10.1038/nmeth900 – start-page: 1 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0275 article-title: structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8M urea publication-title: Biochemistry – volume: 27 start-page: 157 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0025 article-title: Protein promiscuity and its implications for biotechnology publication-title: Nat. Biotechnol. doi: 10.1038/nbt1519 – volume: 134 start-page: 2555 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0330 article-title: Microsecond time-scale conformational exchange in proteins: using long molecular dynamics trajectory to simulate NMR relaxation dispersion data publication-title: J. Am. Chem. Soc. doi: 10.1021/ja206442c – volume: 131 start-page: 6048 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0200 article-title: Accurate sampling of high-frequency motions in proteins by steady-state 15N−{1H} nuclear Overhauser effect measurements in the presence of cross-correlated relaxation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja809526q – volume: 5 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0230 article-title: Nucleophosmin integrates within the nucleolus via multi-modal interactions with proteins displaying R-rich linear motifs and rRNA publication-title: elife doi: 10.7554/eLife.13571 – volume: 143 start-page: 45 year: 2000 ident: 10.1016/j.bbagen.2017.08.020_bb0135 article-title: Cross-correlated relaxation for the measurement of angles between Tensorial interactions publication-title: J. Magn. Reson. doi: 10.1006/jmre.1999.1980 – volume: 12 start-page: 713 year: 1999 ident: 10.1016/j.bbagen.2017.08.020_bb0465 article-title: Folding funnels and binding mechanisms publication-title: Protein Eng. doi: 10.1093/protein/12.9.713 – volume: 6 start-page: 1536 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb1010 article-title: NMR spectroscopy of paramagnetic metalloproteins publication-title: Chembiochem doi: 10.1002/cbic.200500124 – volume: 699 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1335 article-title: Protein NMR structure refinement based on Bayesian inference publication-title: J. Phys. Conf. Ser. doi: 10.1088/1742-6596/699/1/012005 – volume: 135 start-page: 14536 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0370 article-title: A simple method to measure protein side-chain mobility using NMR chemical shifts publication-title: J. Am. Chem. Soc. doi: 10.1021/ja407509z – volume: 41 start-page: 214 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0045 article-title: Characterization of enzyme motions by solution NMR relaxation dispersion publication-title: Acc. Chem. Res. doi: 10.1021/ar700132n – volume: 112 start-page: 8817 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0720 article-title: Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1510083112 – volume: 122 start-page: 5105 year: 2000 ident: 10.1016/j.bbagen.2017.08.020_bb0525 article-title: Ubiquitin backbone motion studied via NH N−C′C αDipolar−dipolar and C′−C′C α/NH NCSA−dipolar cross-correlated relaxation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja993845n – volume: 7 start-page: 2821 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1235 article-title: In-cell protein structures from 2D NMR experiments publication-title: J. Phys. Chem. Lett. doi: 10.1021/acs.jpclett.6b01074 – volume: 131 start-page: 9239 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0775 article-title: Real-time NMR investigations of structural changes in silicon electrodes for lithium-ion batteries publication-title: J. Am. Chem. Soc. doi: 10.1021/ja8086278 – volume: 38 start-page: 129 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb1110 article-title: Automated structure determination from NMR spectra publication-title: Eur. Biophys. J. doi: 10.1007/s00249-008-0367-z – volume: 6 start-page: 38312 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1340 article-title: Improved in-cell structure determination of proteins at near-physiological concentration publication-title: Sci Rep doi: 10.1038/srep38312 – volume: 117 start-page: 139 year: 2017 ident: 10.1016/j.bbagen.2017.08.020_bb0110 article-title: GPCR dynamics: structures in motion publication-title: Chem. Rev. doi: 10.1021/acs.chemrev.6b00177 – volume: 62 start-page: 105 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0990 article-title: Efficient and generalized processing of multidimensional NUS NMR data: the NESTA algorithm and comparison of regularization terms publication-title: J. Biomol. NMR doi: 10.1007/s10858-015-9923-x – volume: 104 start-page: 3623 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb0210 article-title: NMR characterization of the dynamics of biomacromolecules publication-title: Chem. Rev. doi: 10.1021/cr030413t – volume: 120 start-page: 7905 year: 1998 ident: 10.1016/j.bbagen.2017.08.020_bb0215 article-title: Longitudinal and transverse 1H-15N dipolar/15N chemical shift anisotropy relaxation interference: unambiguous determination of rotational diffusion tensors and chemical Exchane effects in biological macromolecules publication-title: J. Am. Chem. Soc. doi: 10.1021/ja980832l – volume: 131 start-page: 16968 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0485 article-title: Toward a unified representation of protein structural dynamics in solution publication-title: J. Am. Chem. Soc. doi: 10.1021/ja907476w – volume: 132 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0910 article-title: Poisson-gap sampling and forward maximum entropy reconstruction for enhancing the resolution and sensitivity of protein NMR data publication-title: J. Am. Chem. Soc. doi: 10.1021/ja908004w – volume: 124 start-page: 10743 year: 2002 ident: 10.1016/j.bbagen.2017.08.020_bb0195 article-title: An NMR experiment for the accurate measurement of heteronuclear spin-lock relaxation rates publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0204776 – volume: 125 start-page: 1731 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb1090 article-title: HADDOCK: a protein-protein docking approach based on biochemical or biophysical information publication-title: J. Am. Chem. Soc. doi: 10.1021/ja026939x – volume: 121 start-page: 1956 year: 1999 ident: 10.1016/j.bbagen.2017.08.020_bb0575 article-title: Determination of RNA sugar pucker mode from cross-correlated relaxation in solution NMR spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja983434r – volume: 14 start-page: 818 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0850 article-title: Selective isotope labelling of leucine residues by using alpha-ketoacid precursor compounds publication-title: Chembiochem doi: 10.1002/cbic.201200737 – volume: 18 start-page: 5839 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0265 article-title: Dynamics of GCN4 facilitate DNA interaction: a model-free analysis of an intrinsically disordered region publication-title: Phys. Chem. Chem. Phys. doi: 10.1039/C5CP06197K – volume: 58 start-page: 287 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0420 article-title: ORIUM: optimized RDC-based iterative and unified model-free analysis publication-title: J. Biomol. NMR doi: 10.1007/s10858-013-9775-1 – volume: 115 start-page: 9832 year: 1993 ident: 10.1016/j.bbagen.2017.08.020_bb0320 article-title: NMR order parameters and free energy: an analytical approach and its application to cooperative Ca2+ binding by Calbindin D9k publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00074a073 – volume: 126 start-page: 5879 year: 2004 ident: 10.1016/j.bbagen.2017.08.020_bb1005 article-title: Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule publication-title: J. Am. Chem. Soc. doi: 10.1021/ja031580d – volume: 30 start-page: 129 year: 2003 ident: 10.1016/j.bbagen.2017.08.020_bb0125 article-title: NMR probes of molecular dynamics: overview and comparison with other techniques publication-title: Annu. Rev. Biophys. Biomol. Struct. doi: 10.1146/annurev.biophys.30.1.129 – volume: 278 start-page: 1111 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb1000 article-title: Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium publication-title: Science doi: 10.1126/science.278.5340.1111 – volume: 134 start-page: 12798 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb1170 article-title: Structure of proteins in eukaryotic compartments publication-title: J. Am. Chem. Soc. doi: 10.1021/ja304809s – volume: 42 start-page: 163 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0290 article-title: Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP publication-title: J. Biomol. NMR doi: 10.1007/s10858-008-9280-0 – volume: 448 start-page: 325 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0315 article-title: Conformational entropy in molecular recognition by proteins publication-title: Nature doi: 10.1038/nature05959 – volume: 467 start-page: 868 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb1140 article-title: The proteasome antechamber maintains substrates in an unfolded state publication-title: Nature doi: 10.1038/nature09444 – volume: 263 start-page: 369 year: 1996 ident: 10.1016/j.bbagen.2017.08.020_bb0310 article-title: Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1996.0581 – volume: 41 start-page: 442 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0610 article-title: Probing invisible, low-populated states of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding publication-title: Acc. Chem. Res. doi: 10.1021/ar700189y – volume: 7 start-page: 553 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0475 article-title: Discovery of selective bioactive small molecules by targeting an RNA dynamic ensemble publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.596 – volume: 134 start-page: 8148 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0705 article-title: Studying “invisible” excited protein states in slow exchange with a major state conformation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja3001419 – volume: 5 start-page: 789 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0065 article-title: The role of dynamic conformational ensembles in biomolecular recognition publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.232 – volume: 69 start-page: 726 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb1095 article-title: HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets publication-title: Proteins doi: 10.1002/prot.21723 – volume: 530 start-page: 45 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1190 article-title: Structural disorder of monomeric alpha-synuclein persists in mammalian cells publication-title: Nature doi: 10.1038/nature16531 – volume: 4 start-page: 849 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0015 article-title: NMR structures of proteins and protein complexes beyond 20,000 M-r publication-title: Nat. Struct. Biol. – volume: 4 start-page: 292 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0405 article-title: NMR evidence for slow collective motions in cyanometmyoglobin publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsb0497-292 – volume: 134 start-page: 4842 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb1280 article-title: Protein crowding affects hydration structure and dynamics publication-title: J. Am. Chem. Soc. doi: 10.1021/ja211115q – volume: 276 start-page: 1230 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0510 article-title: Direct measurement of angles between bond vectors in high-resolution NMR publication-title: Science doi: 10.1126/science.276.5316.1230 – volume: 138 start-page: 6240 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0270 article-title: Identification of dynamic modes in an intrinsically disordered protein using temperature-dependent NMR relaxation publication-title: J. Am. Chem. Soc. doi: 10.1021/jacs.6b02424 – volume: 52 start-page: 11410 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0240 article-title: Predicting the rotational tumbling of dynamic multidomain proteins and supramolecular complexes publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.201305094 – volume: 440 start-page: 52 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0865 article-title: Optimal isotope labelling for NMR protein structure determinations publication-title: Nature doi: 10.1038/nature04525 – volume: 130 start-page: 15361 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0040 article-title: Structural reorganization and preorganization in enzyme active sites: comparisons of experimental and theoretically ideal active site geometries in the multistep serine esterase reaction cycle publication-title: J. Am. Chem. Soc. doi: 10.1021/ja803213p – volume: 83 start-page: 1177 year: 2002 ident: 10.1016/j.bbagen.2017.08.020_bb1040 article-title: Quaternary structure built from subunits combining NMR and small-angle X-ray scattering data publication-title: Biophys. J. doi: 10.1016/S0006-3495(02)75241-7 – volume: 113 start-page: E6939 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0105 article-title: Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1611418113 – volume: 40 start-page: 1339 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0470 article-title: Understanding biomolecular motion, recognition, and allostery by use of conformational ensembles publication-title: Eur. Biophys. J. doi: 10.1007/s00249-011-0754-8 – volume: 7 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0070 article-title: Binding induced conformational changes of proteins correlate with their intrinsic fluctuations: a case study of antibodies publication-title: BMC Struct. Biol. doi: 10.1186/1472-6807-7-31 – volume: 73 start-page: 69 year: 1987 ident: 10.1016/j.bbagen.2017.08.020_bb0905 article-title: Exponential sampling, an alternative method for sampling in two-dimensional Nmr experiments publication-title: J. Magn. Reson. – volume: 12 start-page: 390 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb1295 article-title: Internal and global protein motion assessed with a fusion construct and in-cell NMR spectroscopy publication-title: Chembiochem doi: 10.1002/cbic.201000610 – volume: 24 start-page: 1714 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0640 article-title: Population shuffling between ground and high energy excited states publication-title: Protein Sci. doi: 10.1002/pro.2797 – volume: 13 start-page: 375 year: 1999 ident: 10.1016/j.bbagen.2017.08.020_bb0540 article-title: Efficient determination of angles subtended by Ca-Ha and N-HN vectors in proteins via dipole-dipole cross-correlation publication-title: J. Biomol. NMR doi: 10.1023/A:1008383205836 – volume: 48 start-page: 35 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0700 article-title: Visualizing transient dark states by NMR spectroscopy publication-title: Q. Rev. Biophys. doi: 10.1017/S0033583514000122 – volume: 102 start-page: 622 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb1065 article-title: Solution NMR-derived global fold of a monomeric 82-kDa enzyme publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0407792102 – volume: 315 start-page: 95 year: 2002 ident: 10.1016/j.bbagen.2017.08.020_bb0450 article-title: Concerted motions in HIV-1 TAR RNA may allow access to bound state conformations: RNA dynamics from NMR residual dipolar couplings publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2001.5235 – volume: 53 start-page: 10941 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0340 article-title: Exploration of conformational spaces of high-mannose-type oligosaccharides by an NMR-validated simulation publication-title: Angew. Chem. Int. Ed. Eng. doi: 10.1002/anie.201406145 – volume: 43 start-page: 111 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0825 article-title: An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein publication-title: J. Biomol. NMR doi: 10.1007/s10858-008-9294-7 – volume: 113 start-page: 1725 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb1290 article-title: In-cell thermodynamics and a new role for protein surfaces publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1518620113 – volume: 133 start-page: 13790 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0570 article-title: NMR cross-correlated relaxation rates reveal ion coordination sites in DNA publication-title: J. Am. Chem. Soc. doi: 10.1021/ja202397p – volume: 53 start-page: 10345 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0725 article-title: Characterizing methyl-bearing side chain contacts and dynamics mediating amyloid β protofibril interactions using 13C methyl-DEST and lifetime line broadening publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.201405180 – volume: 18 start-page: 11904 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0165 article-title: Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy publication-title: Molecules (Basel, Switzerland) doi: 10.3390/molecules181011904 – volume: 33 start-page: 3390 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb1080 article-title: Protein length in eukaryotic and prokaryotic proteomes publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki615 – volume: 5 start-page: 1051 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb1320 article-title: NMR protein structure determination in living E. coli cells using nonlinear sampling publication-title: Nat. Protoc. doi: 10.1038/nprot.2010.69 – volume: 178 start-page: 72 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0225 article-title: Effective rotational correlation times of proteins from NMR relaxation interference publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2005.08.014 – volume: 276 start-page: 939 year: 1998 ident: 10.1016/j.bbagen.2017.08.020_bb0550 article-title: A study of protein side-chain dynamics from new 2H auto-correlation and 13C cross-correlation NMR experiments: application to the N-terminal SH3 domain from drk publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1997.1588 – volume: 24 start-page: 706 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb1300 article-title: Hydrogen exchange of disordered proteins in Escherichia coli publication-title: Protein Sci. doi: 10.1002/pro.2643 – volume: 7 start-page: 191 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0670 article-title: Relaxation dispersion NMR spectroscopy for the study of protein allostery publication-title: Biophys. Rev. doi: 10.1007/s12551-015-0166-6 – volume: 470 start-page: 498 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0680 article-title: Transient Hoogsteen base pairs in canonical duplex DNA publication-title: Nature doi: 10.1038/nature09775 – volume: 9 start-page: 462 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0085 article-title: Allosteric inhibition through suppression of transient conformational states publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.1250 – volume: 328 start-page: 98 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb1135 article-title: Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR publication-title: Science doi: 10.1126/science.1184991 – volume: 109 start-page: E3454 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb1150 article-title: Proteasome allostery as a population shift between interchanging conformers publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1213640109 – volume: 102 start-page: 18908 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb0020 article-title: Structural changes involved in protein binding correlate with intrinsic motions of proteins in the unbound state publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.0507603102 – volume: 9 start-page: 297 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1205 article-title: Atomic-resolution monitoring of protein maturation in live human cells by NMR publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.1202 – volume: 6 start-page: 83 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0005 article-title: An empirical framework for binary interactome mapping publication-title: Nat. Methods doi: 10.1038/nmeth.1280 – year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb0385 – volume: 9 start-page: 287 year: 1998 ident: 10.1016/j.bbagen.2017.08.020_bb0180 article-title: Rotational diffusion anisotropy of proteins from simultaneous analysis of publication-title: J. Biomol. NMR doi: 10.1023/A:1018631009583 – volume: 129 start-page: 5108 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0930 article-title: Ultrahigh-resolution H-1-C-13 HSQC spectra of metabolite mixtures using nonlinear sampling and forward maximum entropy reconstruction publication-title: J. Am. Chem. Soc. doi: 10.1021/ja068541x – volume: 131 start-page: 4648 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0955 article-title: Spectroscopy by integration of frequency and time domain information for fast acquisition of high-resolution dark spectra publication-title: J. Am. Chem. Soc. doi: 10.1021/ja807893k – volume: 153 start-page: 293 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0055 article-title: Allostery in disease and in drug discovery publication-title: Cell doi: 10.1016/j.cell.2013.03.034 – volume: 54 start-page: 207 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0605 article-title: Population shuffling of protein conformations publication-title: Angew. Chem. Int. Ed. Eng. doi: 10.1002/anie.201408890 – volume: 104 start-page: 18473 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0690 article-title: Measurement of bond vector orientations in invisible excited states of proteins publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0708296104 – volume: 23 start-page: 1596 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0350 article-title: NMR characterization of the conformational fluctuations of the human lymphocyte function-associated antigen-1 I-domain publication-title: Protein Sci. doi: 10.1002/pro.2538 – volume: 94 start-page: 12366 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0880 article-title: Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.94.23.12366 – volume: 97 start-page: 495 year: 1979 ident: 10.1016/j.bbagen.2017.08.020_bb1370 article-title: Polymerization of the bacterial elongation factor for protein synthesis, EF-Tu publication-title: Eur. J. Biochem. doi: 10.1111/j.1432-1033.1979.tb13137.x – volume: 119 start-page: 6672 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0430 article-title: Locally anisotropic internal polypeptide backbone dynamics by NMR relaxation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja9708676 – volume: 14 start-page: 277 year: 1999 ident: 10.1016/j.bbagen.2017.08.020_bb0545 article-title: Simultaneous determination of psi and phi angles in proteins from measurements of cross-correlated relaxation effects publication-title: J. Biomol. NMR doi: 10.1023/A:1008339928400 – volume: 62 start-page: 373 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0795 article-title: An economic approach to efficient isotope labeling in insect cells using homemade 15N-, 13C- and 2H-labeled yeast extracts publication-title: J. Biomol. NMR doi: 10.1007/s10858-015-9954-3 – volume: 133 start-page: 10336 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0590 article-title: Weak long-range correlated motions in a surface patch of ubiquitin involved in molecular recognition publication-title: J. Am. Chem. Soc. doi: 10.1021/ja200461n – volume: 102 start-page: 13885 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb0435 article-title: Identification of slow correlated motions in proteins using residual dipolar and hydrogen-bond scalar couplings publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.0505129102 – volume: 68 start-page: 101 year: 2017 ident: 10.1016/j.bbagen.2017.08.020_bb0995 article-title: Sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction of both non-uniformly sampled and conventional NMR data publication-title: J. Biomol. NMR doi: 10.1007/s10858-016-0072-7 – volume: 480 start-page: 268 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0715 article-title: Atomic-resolution dynamics on the surface of amyloid-b protofibrils probed by solution NMR publication-title: Nature doi: 10.1038/nature10577 – volume: 47 start-page: 708 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0925 article-title: Nonuniform sampling and maximum entropy reconstruction in multidimensional NMR publication-title: Acc. Chem. Res. doi: 10.1021/ar400244v – volume: 109 start-page: 4108 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb1035 article-title: Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes publication-title: Chem. Rev. doi: 10.1021/cr900033p – volume: 134 start-page: 6365 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0380 article-title: Interpreting protein structural dynamics from NMR chemical shifts publication-title: J. Am. Chem. Soc. doi: 10.1021/ja300265w – volume: 37 start-page: 225 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0790 article-title: Improving cell-free protein synthesis for stable-isotope labeling publication-title: J. Biomol. NMR doi: 10.1007/s10858-006-9127-5 – volume: 46 start-page: 1152 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0445 article-title: A physical picture of atomic motions within the Dickerson DNA dodecamer in solution derived from joint ensemble refinement against NMR and large-angle X-ray scattering data publication-title: Biochemistry doi: 10.1021/bi061943x – volume: 445 start-page: 618 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb1125 article-title: Quantitative dynamics and binding studies of the 20S proteasome by NMR publication-title: Nature doi: 10.1038/nature05512 – volume: 110 start-page: 12867 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0030 article-title: NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1305688110 – volume: 55 start-page: 239 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1305 article-title: Probing non-specific interactions of Ca(2)(+)-calmodulin in E. coli lysate publication-title: J. Biomol. NMR doi: 10.1007/s10858-013-9705-2 – volume: 134 start-page: 12817 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb1330 article-title: A new algorithm for reliable and general NMR resonance assignment publication-title: J. Am. Chem. Soc. doi: 10.1021/ja305091n – volume: 268 start-page: 886 year: 1995 ident: 10.1016/j.bbagen.2017.08.020_bb0245 article-title: Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling publication-title: Science doi: 10.1126/science.7754375 – volume: 131 start-page: 756 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb1115 article-title: Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR publication-title: Cell doi: 10.1016/j.cell.2007.09.039 – volume: 128 start-page: 951 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0760 article-title: Real-time monitoring of chemical transformations by ultrafast 2D NMR spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0564158 – volume: 123 start-page: 2446 year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb1165 article-title: High-resolution macromolecular NMR spectroscopy inside living cells publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0057528 – volume: 508 start-page: 331 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0050 article-title: The ensemble nature of allostery publication-title: Nature doi: 10.1038/nature13001 – volume: 26 start-page: 597 year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb1260 article-title: Macromolecular crowding: obvious but underappreciated publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(01)01938-7 – volume: 39 start-page: 2892 year: 1963 ident: 10.1016/j.bbagen.2017.08.020_bb0710 article-title: Study of moderately rapid chemical exchange reactions by means of nuclear magnetic double resonance publication-title: J. Chem. Phys. doi: 10.1063/1.1734121 – volume: 98 start-page: 3185 year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb1250 article-title: Delivery of proteins into living cells by reversible membrane permeabilization with streptolysin-O publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.051429498 – volume: 116 start-page: 6424 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0120 article-title: Dynamic protein interaction networks and new structural paradigms in signaling publication-title: Chem. Rev. doi: 10.1021/acs.chemrev.5b00548 – volume: 488 start-page: 236 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0325 article-title: Protein activity regulation by conformational entropy publication-title: Nature doi: 10.1038/nature11271 – volume: 112 start-page: 11565 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb1060 article-title: Dynamic equilibrium between closed and partially closed states of the bacterial enzyme I unveiled by solution NMR and X-ray scattering publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.1515366112 – volume: 138 start-page: 8412 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0595 article-title: Direct investigation of slow correlated dynamics in proteins via dipolar interactions publication-title: J. Am. Chem. Soc. doi: 10.1021/jacs.6b01447 – volume: 450 start-page: 1263 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0345 article-title: Visualizing spatially correlated dynamics that directs RNA conformational transitions publication-title: Nature doi: 10.1038/nature06389 – volume: 28 start-page: 8972 year: 1989 ident: 10.1016/j.bbagen.2017.08.020_bb0150 article-title: Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease publication-title: Biochemistry doi: 10.1021/bi00449a003 – volume: 50 start-page: 6548 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0975 article-title: Fast multidimensional NMR spectroscopy using compressed sensing publication-title: Angew. Chem. Int. Ed. Eng. doi: 10.1002/anie.201100440 – volume: 106 start-page: 1720 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb0390 article-title: NMR residual dipolar couplings as probes of biomolecular dynamics publication-title: Chem. Rev. doi: 10.1021/cr040429z – volume: 120 start-page: 10571 year: 1998 ident: 10.1016/j.bbagen.2017.08.020_bb1020 article-title: Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses publication-title: J. Am. Chem. Soc. doi: 10.1021/ja982592f – volume: 127 start-page: 16621 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb1045 article-title: Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data publication-title: J. Am. Chem. Soc. doi: 10.1021/ja054342m – volume: 116 start-page: 8426 year: 1994 ident: 10.1016/j.bbagen.2017.08.020_bb0425 article-title: NMR order parameters of biomolecules: a new analytical representation and application to the Gaussian axial fluctuation model publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00097a084 – volume: 2 start-page: 865 year: 1995 ident: 10.1016/j.bbagen.2017.08.020_bb0755 article-title: Following protein folding in real time using NMR spectroscopy publication-title: Nat. Struct. Biol. doi: 10.1038/nsb1095-865 – volume: 273 start-page: 283 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb1105 article-title: Torsion angle dynamics for NMR structure calculation with the new program DYANA publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1997.1284 – volume: 131 start-page: 10834 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb1220 article-title: Observation of NMR signals from proteins introduced into living mammalian cells by reversible membrane permeabilization using a pore-forming toxin, streptolysin o publication-title: J. Am. Chem. Soc. doi: 10.1021/ja904407w – volume: 426 start-page: 3214 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb1310 article-title: A similar in vitro and in cell lysate folding intermediate for the FF domain publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2014.07.019 – volume: 52 start-page: 1208 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb1345 article-title: A gel-encapsulated bioreactor system for NMR studies of protein-protein interactions in living mammalian cells publication-title: Angew. Chem. Int. Ed. Eng. doi: 10.1002/anie.201207243 – volume: 113 start-page: 3269 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0645 article-title: Allosteric switch regulates protein–protein binding through collective motion publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1519609113 – volume: 68 start-page: 14 year: 1986 ident: 10.1016/j.bbagen.2017.08.020_bb0920 article-title: Reconstruction of phase sensitive 2D NMR spectra by maximum entropy publication-title: J. Magn. Reson. – start-page: 1 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb0100 – volume: 300 start-page: 197 year: 2000 ident: 10.1016/j.bbagen.2017.08.020_bb1075 article-title: Global folds of proteins with low densities of NOEs using residual dipolar couplings: application to the 370-residue maltodextrin-binding protein publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.3842 – volume: 133 start-page: 11154 year: 2011 ident: 10.1016/j.bbagen.2017.08.020_bb0740 article-title: Transient enzyme–substrate recognition monitored by real-time NMR publication-title: J. Am. Chem. Soc. doi: 10.1021/ja2010048 – volume: 122 start-page: 12728 year: 2000 ident: 10.1016/j.bbagen.2017.08.020_bb0560 article-title: NMR spectroscopic determination of angles α and ζ in RNA from CH-dipolar coupling, P-CSA cross-correlated relaxation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja001432c – volume: 41 start-page: 139 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0250 article-title: Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics publication-title: J. Biomol. NMR doi: 10.1007/s10858-008-9244-4 – volume: 67 start-page: 23 year: 2017 ident: 10.1016/j.bbagen.2017.08.020_bb0860 article-title: Bacterial production of site specific 13C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins publication-title: J. Biomol. NMR doi: 10.1007/s10858-016-0081-6 – volume: 58 start-page: 129 year: 2014 ident: 10.1016/j.bbagen.2017.08.020_bb0950 article-title: Time-resolved multidimensional NMR with non-uniform sampling publication-title: J. Biomol. NMR doi: 10.1007/s10858-013-9811-1 – volume: 320 start-page: 1471 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0075 article-title: Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution publication-title: Science doi: 10.1126/science.1157092 – volume: 239 start-page: 79 year: 1994 ident: 10.1016/j.bbagen.2017.08.020_bb0395 article-title: Measurement of homo- and heteronuclear J couplings from quantitative J correlation publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(94)39004-5 – volume: 132 start-page: 10992 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0660 article-title: 13CHD 2Methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics publication-title: J. Am. Chem. Soc. doi: 10.1021/ja104578n – volume: 40 start-page: 199 year: 2002 ident: 10.1016/j.bbagen.2017.08.020_bb0130 article-title: Semi-classical nuclear spin relaxation theory revisited for use with biological macromolecules publication-title: Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/S0079-6565(01)00043-7 – volume: 129 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0835 article-title: A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0761784 – volume: 127 start-page: 14970 year: 2005 ident: 10.1016/j.bbagen.2017.08.020_bb0375 article-title: A simple method to predict protein flexibility using secondary chemical shifts publication-title: J. Am. Chem. Soc. doi: 10.1021/ja054842f – volume: 129 start-page: 13396 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb0695 article-title: Characterization of chemical exchange using residual dipolar coupling publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0761636 – volume: 192 start-page: 123 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0915 article-title: Optimization of random time domain sampling in multidimensional NMR publication-title: J. Magn. Reson. doi: 10.1016/j.jmr.2008.02.003 – volume: 128 start-page: 9719 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0440 article-title: Kinetics of the antibody recognition site in the third IgG-binding domain of protein G publication-title: Angew. Chem. doi: 10.1002/ange.201603501 – volume: 40 start-page: 95 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb1055 article-title: Refined solution structure of the 82-kDa enzyme malate synthase G from joint NMR and synchrotron SAXS restraints publication-title: J. Biomol. NMR doi: 10.1007/s10858-007-9211-5 – volume: 131 start-page: 3668 year: 2009 ident: 10.1016/j.bbagen.2017.08.020_bb0520 article-title: Correlated dynamics between protein HN and HC bonds observed by NMR cross relaxation publication-title: J. Am. Chem. Soc. doi: 10.1021/ja808616v – volume: 103 start-page: 11904 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb1175 article-title: Quantitative NMR analysis of the protein G B1 domain in Xenopus laevis egg extracts and intact oocytes publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0604667103 – volume: 119 start-page: 7599 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0815 article-title: Production and incorporation of N-15, C-13, H-2 (H-1-delta 1 methyl) isoleucine into proteins for multidimensional NMR studies publication-title: J. Am. Chem. Soc. doi: 10.1021/ja9706514 – volume: 35 start-page: 313 year: 2006 ident: 10.1016/j.bbagen.2017.08.020_bb1050 article-title: A target function for quaternary structural refinement from small angle scattering and NMR orientational restraints publication-title: Eur. Biophys. J. doi: 10.1007/s00249-005-0037-3 – volume: 4 start-page: 443 year: 1997 ident: 10.1016/j.bbagen.2017.08.020_bb0160 article-title: Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsb0697-443 – volume: 8 start-page: 926 year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb0305 article-title: Dynamic activation of protein function: a view emerging from NMR spectroscopy publication-title: Nat. Struct. Biol. doi: 10.1038/nsb1101-926 – volume: 54 start-page: 5328 year: 2015 ident: 10.1016/j.bbagen.2017.08.020_bb1350 article-title: Direct observation of Ca(2+) -induced calmodulin conformational transitions in intact Xenopus laevis oocytes by (19) F NMR spectroscopy publication-title: Angew. Chem. Int. Ed. Eng. doi: 10.1002/anie.201500261 – volume: 135 start-page: 5457 year: 2013 ident: 10.1016/j.bbagen.2017.08.020_bb0455 article-title: A general method for constructing atomic-resolution RNA ensembles using NMR residual dipolar couplings: the basis for interhelical motions revealed publication-title: J. Am. Chem. Soc. doi: 10.1021/ja400920w – volume: 123 start-page: 6098 year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb0410 article-title: Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins publication-title: J. Am. Chem. Soc. doi: 10.1021/ja010002z – volume: 66 start-page: 37 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0875 article-title: C-13-NMR studies on disulfide bond isomerization in bovine pancreatic trypsin inhibitor (BPTI) publication-title: J. Biomol. NMR doi: 10.1007/s10858-016-0055-8 – volume: 52 start-page: 315 year: 2012 ident: 10.1016/j.bbagen.2017.08.020_bb0985 article-title: Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional poisson gap scheduling publication-title: J. Biomol. NMR doi: 10.1007/s10858-012-9611-z – volume: 129 start-page: 1743 year: 2007 ident: 10.1016/j.bbagen.2017.08.020_bb1130 article-title: Probing side-chain dynamics in the proteasome by relaxation violated coherence transfer NMR spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja067827z – volume: 98 start-page: 7684 year: 2001 ident: 10.1016/j.bbagen.2017.08.020_bb0360 article-title: Functional dynamics in the active site of the ribonuclease binase publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.121069998 – volume: 120 start-page: 8313 year: 2016 ident: 10.1016/j.bbagen.2017.08.020_bb0335 article-title: Picosecond to millisecond structural dynamics in human ubiquitin publication-title: J. Phys. Chem. B doi: 10.1021/acs.jpcb.6b02024 – volume: 276 start-page: 657 year: 1998 ident: 10.1016/j.bbagen.2017.08.020_bb0765 article-title: Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1997.1553 – volume: 124 start-page: 12020 year: 2002 ident: 10.1016/j.bbagen.2017.08.020_bb0415 article-title: A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0261123 – volume: 47 start-page: 5235 year: 2008 ident: 10.1016/j.bbagen.2017.08.020_bb0785 article-title: Time-resolved dynamic nuclear polarization enhanced NMR spectroscopy publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.200801492 – volume: 13 start-page: 527 year: 2010 ident: 10.1016/j.bbagen.2017.08.020_bb0095 article-title: Conformational ensembles, signal transduction and residue hot spots: application to drug discovery publication-title: Curr. Opin. Drug Discov. Devel. |
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| Snippet | To understand the mechanisms related to the ‘dynamical ordering’ of macromolecules and biological systems, it is crucial to monitor, in detail, molecular... To understand the mechanisms related to the 'dynamical ordering' of macromolecules and biological systems, it is crucial to monitor, in detail, molecular... |
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| SubjectTerms | Dynamical ordering Dynamics homeostasis human diseases In-cell NMR Large biomacromolecules nuclear magnetic resonance spectroscopy proteins Solution NMR spectroscopy Stable isotope labelling thermodynamics |
| Title | Solution NMR views of dynamical ordering of biomacromolecules |
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