A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations
Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted t...
Saved in:
| Published in | Biophysical journal Vol. 97; no. 10; pp. 2803 - 2810 |
|---|---|
| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
15.11.2009
Biophysical Society The Biophysical Society |
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the ββα zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal β-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41°C may be a reflection of the melting of its α-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered. |
|---|---|
| AbstractList | Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the beta beta alpha zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal beta -hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41 degree C may be a reflection of the melting of its alpha -helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered. Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the ββα zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal β-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41...C may be a reflection of the melting of its ...-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered. (ProQuest: ... denotes formulae/symbols omitted.) Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the betabetaalpha zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal beta-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41 degrees C may be a reflection of the melting of its alpha-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered. Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the ββα zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal β -hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41°C may be a reflection of the melting of its α -helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered. Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations possible. However, not all mini-proteins are created equal. The stability and structure of FSD-1, a 28-residue mini-protein that adopted the ββα zinc-finger motif independent of zinc binding, was investigated using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The broad melting transition of FSD-1, similar to that of a helix-to-coil transition, was observed by using circular dichroism, differential scanning calorimetry, and replica-exchange molecular dynamics. The N-terminal β-hairpin was found to be flexible. The FSD-1 apparent melting temperature of 41°C may be a reflection of the melting of its α-helical segment instead of the entire protein. Thus, despite its attractiveness due to small size and purposefully designed helix, sheet, and turn structures, the status of FSD-1 as a model system for studying protein folding should be reconsidered. |
| Author | Marshall, Garland R. Feng, Jianwen A. Kao, Jeff |
| AuthorAffiliation | Center for Computational Biology, Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, Missouri Department of Chemistry, Washington University in St. Louis, St. Louis, Missouri |
| AuthorAffiliation_xml | – name: Department of Chemistry, Washington University in St. Louis, St. Louis, Missouri – name: Center for Computational Biology, Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, Missouri |
| Author_xml | – sequence: 1 givenname: Jianwen A. surname: Feng fullname: Feng, Jianwen A. email: jafeng@artsci.wustl.edu organization: Center for Computational Biology, Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, Missouri – sequence: 2 givenname: Jeff surname: Kao fullname: Kao, Jeff organization: Department of Chemistry, Washington University in St. Louis, St. Louis, Missouri – sequence: 3 givenname: Garland R. surname: Marshall fullname: Marshall, Garland R. organization: Center for Computational Biology, Department of Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, Missouri |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19917235$$D View this record in MEDLINE/PubMed |
| BookMark | eNp9ks1uEzEUhS1URNPAA7BBFhtYdMK945-ZAQkpSikgBYEUurY8Hk_rMLGDPamUJ-C1cUnE36IrW_J3js-9OmfkxAdvCXmKMENA-Wo9a7frWQnQzKCeAZcPyAQFLwuAWp6QCQDIgvFGnJKzlNYAWArAR-QUmwarkokJ-TGnK2uC7-gyhG9Uj_ST8674EsNonaerUbducOP-NZ17PeyTSzT09HJ1USC9Ss5f04WLZjfoSC-cuYnBpc15vva9jdaPTg90ZbT3v0g9hOg2doz7c6rzlyu3ycrRBZ8ek4e9HpJ9cjyn5Ory3dfFh2L5-f3HxXxZGIEwFnUP3NQ1QyaMaE2lS2HrlrVo-77VnTHYCl7z1jSNaaVkwpZdw2uNwCSHumFT8vbgu921G9uZnDHqQW1zLh33Kmin_n3x7kZdh1tVVpUsG5kNXhwNYvi-s2lUG5eMHQbtbdglVTGOvISccEpe3kuirJBxhlhl9Pl_6DrsYl54UiUK2VQVsAzhATIxpBRt_zs1grrrg1qr3Ad11wcFtcp9yJpnf4_7R3EsQAbeHACbl37rbFTJOOuN7Vy0ZlRdcPfY_wTV-chN |
| CitedBy_id | crossref_primary_10_1371_journal_pcbi_1000998 crossref_primary_10_1073_pnas_1812756115 crossref_primary_10_5012_bkcs_2014_35_6_1713 crossref_primary_10_1038_ncomms6330 crossref_primary_10_3390_ijms11104014 crossref_primary_10_1007_s10989_016_9545_5 crossref_primary_10_1016_j_bmc_2015_03_058 crossref_primary_10_1021_ct200094b crossref_primary_10_1038_ncomms15443 crossref_primary_10_1021_acs_jpcb_6b08883 crossref_primary_10_1021_jp300074f |
| Cites_doi | 10.1007/s10989-006-9058-8 10.1002/prot.21312 10.1002/prot.20771 10.1016/j.jmb.2003.11.027 10.1073/pnas.1330954100 10.1016/S0076-6879(04)83012-X 10.1006/jmbi.2000.4345 10.1063/1.1822916 10.1073/pnas.88.7.2854 10.1006/jmbi.1999.3025 10.1073/pnas.97.7.3034 10.1146/annurev.biophys.34.040204.144447 10.1126/science.271.5247.342 10.1093/protein/13.7.501 10.1002/prot.1167 10.1021/jp0757715 10.1016/S1359-0278(98)00015-7 10.1126/science.278.5335.82 10.1021/bi00421a014 10.1063/1.2056540 10.1021/ja8030533 10.1002/bip.360311304 10.1021/jp063716a 10.1016/0076-6879(95)59042-0 10.1021/bi00699a001 10.1016/j.bpc.2004.12.040 10.1016/S0009-2614(99)01123-9 10.1016/j.jmb.2005.09.030 10.1002/jcc.20291 |
| ContentType | Journal Article |
| Copyright | 2009 Biophysical Society Copyright Biophysical Society Nov 15, 2009 2009 by the Biophysical Society.. 2009 Biophysical Society |
| Copyright_xml | – notice: 2009 Biophysical Society – notice: Copyright Biophysical Society Nov 15, 2009 – notice: 2009 by the Biophysical Society.. 2009 Biophysical Society |
| DBID | 6I. AAFTH CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QO 7QP 7TK 7TM 7U9 8FD FR3 H94 K9. P64 7TB 7U5 L7M 7X8 5PM |
| DOI | 10.1016/j.bpj.2009.08.046 |
| DatabaseName | ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Biotechnology Research Abstracts Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Nucleic Acids Abstracts Virology and AIDS Abstracts Technology Research Database Engineering Research Database AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) Biotechnology and BioEngineering Abstracts Mechanical & Transportation Engineering Abstracts Solid State and Superconductivity Abstracts Advanced Technologies Database with Aerospace MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Virology and AIDS Abstracts Biotechnology Research Abstracts Technology Research Database Nucleic Acids Abstracts AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) Engineering Research Database Calcium & Calcified Tissue Abstracts Neurosciences Abstracts Biotechnology and BioEngineering Abstracts Solid State and Superconductivity Abstracts Mechanical & Transportation Engineering Abstracts Advanced Technologies Database with Aerospace MEDLINE - Academic |
| DatabaseTitleList | Solid State and Superconductivity Abstracts Virology and AIDS Abstracts MEDLINE |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Biology |
| EISSN | 1542-0086 |
| EndPage | 2810 |
| ExternalDocumentID | 1907739161 10_1016_j_bpj_2009_08_046 19917235 S0006349509014398 |
| Genre | Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R01 GM068460 – fundername: NIGMS NIH HHS grantid: T32 GM008802 – fundername: NIGMS NIH HHS grantid: GM 008802 |
| GroupedDBID | --- --K -DZ -~X .55 0R~ 23N 2WC 4.4 457 53G 5GY 5RE 62- 6I. 6J9 6TJ AACTN AAEDT AAEDW AAFTH AAIAV AAIKJ AAKRW AALRI AAUCE AAVLU AAXJY AAXUO ABJNI ABMAC ABMWF ABVKL ACBEA ACGFO ACGFS ACGOD ACIWK ACNCT ACPRK ADBBV ADEZE ADJPV AENEX AEXQZ AFRAH AFTJW AGHFR AGKMS AHMBA AHPSJ AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ AOIJS AYCSE AZFZN BAWUL CS3 D0L DIK DU5 E3Z EBS EJD F5P FCP FDB FRP GX1 HYE HZ~ IH2 IXB JIG KQ8 L7B M41 N9A NCXOZ O-L O9- OK1 P2P RCE RIG RNS ROL RPM RWL SES SSZ TAE TBP TN5 WH7 WOQ WOW WQ6 X7M YNY YWH ZA5 ~02 0SF AAMRU ADVLN AKAPO AKRWK ALIPV CGR CUY CVF ECM EIF NPM .GJ 3O- 3V. 7X2 7X7 88A 88E 88I 8AF 8AO 8FE 8FG 8FH 8FI 8FJ 8G5 8R4 8R5 AAQXK AAYXX ABUWG ACRPL ADMUD ADNMO AFKRA AI. ARAPS ASPBG ATCPS AVWKF AZQEC BBNVY BENPR BGLVJ BHPHI BPHCQ BVXVI CCPQU CITATION DWQXO FEDTE FGOYB FYUFA G-2 GNUQQ GUQSH H13 HCIFZ HMCUK HVGLF HX~ LK8 M0K M0L M1P M2O M2P M2Q M7P MVM OZT P62 PQQKQ PRG PROAC PSQYO Q2X R2- S0X UKHRP UKR VH1 YYP ZGI ZXP ~KM 7QO 7QP 7TK 7TM 7U9 8FD FR3 H94 K9. P64 7TB 7U5 L7M 7X8 5PM |
| ID | FETCH-LOGICAL-c510t-8f04c883135c5bc7a25e8b3b1effbadcc1b5484bc99cb6635e2d948a103640893 |
| IEDL.DBID | RPM |
| ISSN | 0006-3495 |
| IngestDate | Tue Sep 17 20:54:13 EDT 2024 Fri Oct 25 10:56:31 EDT 2024 Fri Oct 25 22:36:25 EDT 2024 Thu Oct 10 19:10:46 EDT 2024 Fri Dec 06 08:42:39 EST 2024 Sat Sep 28 07:45:41 EDT 2024 Fri Feb 23 02:37:23 EST 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 10 |
| Language | English |
| License | http://www.elsevier.com/open-access/userlicense/1.0 This document may be redistributed and reused, subject to certain conditions. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c510t-8f04c883135c5bc7a25e8b3b1effbadcc1b5484bc99cb6635e2d948a103640893 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
| OpenAccessLink | https://www.sciencedirect.com/science/article/pii/S0006349509014398 |
| PMID | 19917235 |
| PQID | 215697703 |
| PQPubID | 7454 |
| PageCount | 8 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_2776296 proquest_miscellaneous_734142031 proquest_miscellaneous_1671343117 proquest_journals_215697703 crossref_primary_10_1016_j_bpj_2009_08_046 pubmed_primary_19917235 elsevier_sciencedirect_doi_10_1016_j_bpj_2009_08_046 |
| PublicationCentury | 2000 |
| PublicationDate | 2009-11-15 |
| PublicationDateYYYYMMDD | 2009-11-15 |
| PublicationDate_xml | – month: 11 year: 2009 text: 2009-11-15 day: 15 |
| PublicationDecade | 2000 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: New York |
| PublicationTitle | Biophysical journal |
| PublicationTitleAlternate | Biophys J |
| PublicationYear | 2009 |
| Publisher | Elsevier Inc Biophysical Society The Biophysical Society |
| Publisher_xml | – name: Elsevier Inc – name: Biophysical Society – name: The Biophysical Society |
| References | Freire (bib22) 1995; 259 Sugita, Okamoto (bib2) 1999; 314 Snow, Sorin, Rhee, Pande (bib1) 2005; 34 Zhang, Wu, Duan (bib24) 2005; 123 Delano (bib33) 2009 Taylor, Greenfield, Wu, Privalov (bib19) 1999; 291 Lei, Duan (bib10) 2004; 121 Karle, Das, Balaram (bib27) 2000; 97 Catlett (bib32) 2007 Godoy-Ruiz, Henry, Kubelka, Hofrichter, Munoz (bib23) 2008; 112 Consalvi, Chiaraluce, Giangiacomo, Scandurra, Christova (bib16) 2000; 13 Honda, Akiba, Kato, Sawada, Sekijima (bib17) 2008; 130 Reference deleted in proof. Sarisky, Mayo (bib26) 2001; 307 Struthers, Ottesen, Imperiali (bib5) 1998; 3 Kim, Lee, Lee (bib13) 2005; 115 Pitera, Swope (bib25) 2003; 100 Struthers, Cheng, Imperiali (bib6) 1996; 271 Roberts (bib28) 1993 Dahiyat, Mayo (bib7) 1997; 278 Santoro, Bolen (bib15) 1988; 27 Greenfield (bib14) 2004; 383 Van Der Spoel, Lindahl, Hess, Groenhof, Mark (bib31) 2005; 26 Lei, Dastidar, Duan (bib9) 2006; 110 Scholtz, Qian, York, Stewart, Baldwin (bib20) 1991; 31 Jang, Kim, Pak (bib12) 2006; 62 Sanbonmatsu, Garcia (bib3) 2002; 46 Seibert, Patriksson, Hess, van der Spoel (bib4) 2005; 354 Feng, Tessler, Marshall (bib8) 2007; 13 Scholtz, Marqusee, Baldwin, York, Stewart (bib18) 1991; 88 Richardson, Makhatadze (bib21) 2004; 335 Chou, Fasman (bib30) 1974; 13 Li, Zhang, Wang (bib11) 2007; 67 15634176 - J Chem Phys. 2004 Dec 15;121(23):12104-11 16211538 - J Comput Chem. 2005 Dec;26(16):1701-18 2011594 - Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2854-8 16329109 - Proteins. 2006 Mar 15;62(3):663-71 10452900 - J Mol Biol. 1999 Aug 27;291(4):965-76 11807951 - Proteins. 2002 Feb 1;46(2):225-34 9311930 - Science. 1997 Oct 3;278(5335):82-7 15869383 - Annu Rev Biophys Biomol Struct. 2005;34:43-69 15063655 - Methods Enzymol. 2004;383:282-317 16236315 - J Mol Biol. 2005 Nov 18;354(1):173-83 14698297 - J Mol Biol. 2004 Jan 23;335(4):1029-37 8538451 - Methods Enzymol. 1995;259:144-68 10725396 - Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3034-7 11292351 - J Mol Biol. 2001 Apr 13;307(5):1411-8 4358939 - Biochemistry. 1974 Jan 15;13(2):211-22 17285627 - Proteins. 2007 May 1;67(2):338-49 1814498 - Biopolymers. 1991 Nov;31(13):1463-70 15752604 - Biophys Chem. 2005 Apr 1;115(2-3):195-200 9565754 - Fold Des. 1998;3(2):95-103 17064170 - J Phys Chem B. 2006 Nov 2;110(43):22001-8 18950166 - J Am Chem Soc. 2008 Nov 19;130(46):15327-31 16252940 - J Chem Phys. 2005 Oct 15;123(15):154105 18278894 - J Phys Chem B. 2008 May 15;112(19):5938-49 8553067 - Science. 1996 Jan 19;271(5247):342-5 3233195 - Biochemistry. 1988 Oct 18;27(21):8063-8 10906345 - Protein Eng. 2000 Jul;13(7):501-7 12808142 - Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7587-92 Godoy-Ruiz (10.1016/j.bpj.2009.08.046_bib23) 2008; 112 Jang (10.1016/j.bpj.2009.08.046_bib12) 2006; 62 Dahiyat (10.1016/j.bpj.2009.08.046_bib7) 1997; 278 Greenfield (10.1016/j.bpj.2009.08.046_bib14) 2004; 383 Van Der Spoel (10.1016/j.bpj.2009.08.046_bib31) 2005; 26 Scholtz (10.1016/j.bpj.2009.08.046_bib20) 1991; 31 Honda (10.1016/j.bpj.2009.08.046_bib17) 2008; 130 Lei (10.1016/j.bpj.2009.08.046_bib10) 2004; 121 Roberts (10.1016/j.bpj.2009.08.046_bib28) 1993 Chou (10.1016/j.bpj.2009.08.046_bib30) 1974; 13 Santoro (10.1016/j.bpj.2009.08.046_bib15) 1988; 27 Scholtz (10.1016/j.bpj.2009.08.046_bib18) 1991; 88 10.1016/j.bpj.2009.08.046_bib29 Li (10.1016/j.bpj.2009.08.046_bib11) 2007; 67 Struthers (10.1016/j.bpj.2009.08.046_bib6) 1996; 271 Sugita (10.1016/j.bpj.2009.08.046_bib2) 1999; 314 Kim (10.1016/j.bpj.2009.08.046_bib13) 2005; 115 Pitera (10.1016/j.bpj.2009.08.046_bib25) 2003; 100 Delano (10.1016/j.bpj.2009.08.046_bib33) 2009 Feng (10.1016/j.bpj.2009.08.046_bib8) 2007; 13 Catlett (10.1016/j.bpj.2009.08.046_bib32) 2007 Freire (10.1016/j.bpj.2009.08.046_bib22) 1995; 259 Zhang (10.1016/j.bpj.2009.08.046_bib24) 2005; 123 Struthers (10.1016/j.bpj.2009.08.046_bib5) 1998; 3 Sarisky (10.1016/j.bpj.2009.08.046_bib26) 2001; 307 Sanbonmatsu (10.1016/j.bpj.2009.08.046_bib3) 2002; 46 Lei (10.1016/j.bpj.2009.08.046_bib9) 2006; 110 Karle (10.1016/j.bpj.2009.08.046_bib27) 2000; 97 Taylor (10.1016/j.bpj.2009.08.046_bib19) 1999; 291 Richardson (10.1016/j.bpj.2009.08.046_bib21) 2004; 335 Consalvi (10.1016/j.bpj.2009.08.046_bib16) 2000; 13 Seibert (10.1016/j.bpj.2009.08.046_bib4) 2005; 354 Snow (10.1016/j.bpj.2009.08.046_bib1) 2005; 34 |
| References_xml | – volume: 26 start-page: 1701 year: 2005 end-page: 1718 ident: bib31 article-title: GROMACS: fast, flexible, and free publication-title: J. Comput. Chem. contributor: fullname: Mark – volume: 115 start-page: 195 year: 2005 end-page: 200 ident: bib13 article-title: Folding simulations of small proteins publication-title: Biophys. Chem. contributor: fullname: Lee – year: 1993 ident: bib28 article-title: NMR of Macromolecules: A Practical Approach contributor: fullname: Roberts – volume: 13 start-page: 501 year: 2000 end-page: 507 ident: bib16 article-title: Thermal unfolding and conformational stability of the recombinant domain II of glutamate dehydrogenase from the hyperthermophile publication-title: Protein Eng. contributor: fullname: Christova – volume: 31 start-page: 1463 year: 1991 end-page: 1470 ident: bib20 article-title: Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water publication-title: Biopolymers contributor: fullname: Baldwin – volume: 27 start-page: 8063 year: 1988 end-page: 8068 ident: bib15 article-title: Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants publication-title: Biochemistry contributor: fullname: Bolen – volume: 291 start-page: 965 year: 1999 end-page: 976 ident: bib19 article-title: A calorimetric study of the folding-unfolding of an alpha-helix with covalently closed N and C-terminal loops publication-title: J. Mol. Biol. contributor: fullname: Privalov – volume: 121 start-page: 12104 year: 2004 end-page: 12111 ident: bib10 article-title: The role of plastic beta-hairpin and weak hydrophobic core in the stability and unfolding of a full sequence design protein publication-title: J. Chem. Phys. contributor: fullname: Duan – year: 2009 ident: bib33 article-title: The PyMOL Molecular Graphics System contributor: fullname: Delano – volume: 314 start-page: 141 year: 1999 end-page: 151 ident: bib2 article-title: Replica-exchange molecular dynamics method for protein folding publication-title: Chem. Phys. Lett. contributor: fullname: Okamoto – volume: 67 start-page: 338 year: 2007 end-page: 349 ident: bib11 article-title: Understanding the folding and stability of a zinc finger-based full sequence design protein with replica exchange molecular dynamics simulations publication-title: Proteins contributor: fullname: Wang – volume: 383 start-page: 282 year: 2004 end-page: 317 ident: bib14 article-title: Analysis of circular dichroism data publication-title: Methods Enzymol. contributor: fullname: Greenfield – volume: 335 start-page: 1029 year: 2004 end-page: 1037 ident: bib21 article-title: Temperature dependence of the thermodynamics of helix-coil transition publication-title: J. Mol. Biol. contributor: fullname: Makhatadze – year: 2007 ident: bib32 article-title: TeraGrid: analysis of organization, system architecture, and middleware enabling new types of applications, HPC and grids in action publication-title: Advances in Parallel Computing contributor: fullname: Catlett – volume: 13 start-page: 151 year: 2007 end-page: 160 ident: bib8 article-title: Chimeric protein engineering publication-title: Int. J. Pept. Res. Ther. contributor: fullname: Marshall – volume: 88 start-page: 2854 year: 1991 end-page: 2858 ident: bib18 article-title: Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Stewart – volume: 112 start-page: 5938 year: 2008 end-page: 5949 ident: bib23 article-title: Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data publication-title: J. Phys. Chem. contributor: fullname: Munoz – volume: 259 start-page: 144 year: 1995 end-page: 168 ident: bib22 article-title: Thermal denaturation methods in the study of protein folding publication-title: Methods Enzymol. contributor: fullname: Freire – volume: 62 start-page: 663 year: 2006 end-page: 671 ident: bib12 article-title: Free energy surfaces of miniproteins with a publication-title: Proteins contributor: fullname: Pak – volume: 278 start-page: 82 year: 1997 end-page: 87 ident: bib7 article-title: De novo protein design: fully automated sequence selection publication-title: Science contributor: fullname: Mayo – volume: 110 start-page: 22001 year: 2006 end-page: 22008 ident: bib9 article-title: Folding transition-state and denatured-state ensembles of FSD-1 from folding and unfolding simulations publication-title: J. Phys. Chem. B contributor: fullname: Duan – volume: 307 start-page: 1411 year: 2001 end-page: 1418 ident: bib26 article-title: The beta-beta-alpha fold: explorations in sequence space publication-title: J. Mol. Biol. contributor: fullname: Mayo – volume: 46 start-page: 225 year: 2002 end-page: 234 ident: bib3 article-title: Structure of Met-enkephalin in explicit aqueous solution using replica exchange molecular dynamics publication-title: Proteins contributor: fullname: Garcia – volume: 97 start-page: 3034 year: 2000 end-page: 3037 ident: bib27 article-title: De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Balaram – volume: 123 start-page: 154105 year: 2005 ident: bib24 article-title: Convergence of replica exchange molecular dynamics publication-title: J. Chem. Phys. contributor: fullname: Duan – volume: 13 start-page: 211 year: 1974 end-page: 222 ident: bib30 article-title: Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins publication-title: Biochemistry contributor: fullname: Fasman – volume: 34 start-page: 43 year: 2005 end-page: 69 ident: bib1 article-title: How well can simulation predict protein folding kinetics and thermodynamics? publication-title: Annu. Rev. Biophys. Biomol. Struct. contributor: fullname: Pande – volume: 271 start-page: 342 year: 1996 end-page: 345 ident: bib6 article-title: Design of a monomeric 23-residue polypeptide with defined tertiary structure publication-title: Science contributor: fullname: Imperiali – volume: 100 start-page: 7587 year: 2003 end-page: 7592 ident: bib25 article-title: Understanding folding and design: replica-exchange simulations of “Trp-cage” miniproteins publication-title: Proc. Natl. Acad. Sci. USA contributor: fullname: Swope – volume: 3 start-page: 95 year: 1998 end-page: 103 ident: bib5 article-title: Design and NMR analyses of compact, independently folded publication-title: Fold. Des. contributor: fullname: Imperiali – volume: 354 start-page: 173 year: 2005 end-page: 183 ident: bib4 article-title: Reproducible polypeptide folding and structure prediction using molecular dynamics simulations publication-title: J. Mol. Biol. contributor: fullname: van der Spoel – volume: 130 start-page: 15327 year: 2008 end-page: 15331 ident: bib17 article-title: Crystal structure of a ten-amino acid protein publication-title: J. Am. Chem. Soc. contributor: fullname: Sekijima – volume: 13 start-page: 151 year: 2007 ident: 10.1016/j.bpj.2009.08.046_bib8 article-title: Chimeric protein engineering publication-title: Int. J. Pept. Res. Ther. doi: 10.1007/s10989-006-9058-8 contributor: fullname: Feng – volume: 67 start-page: 338 year: 2007 ident: 10.1016/j.bpj.2009.08.046_bib11 article-title: Understanding the folding and stability of a zinc finger-based full sequence design protein with replica exchange molecular dynamics simulations publication-title: Proteins doi: 10.1002/prot.21312 contributor: fullname: Li – volume: 62 start-page: 663 year: 2006 ident: 10.1016/j.bpj.2009.08.046_bib12 article-title: Free energy surfaces of miniproteins with a ββα motif: replica exchange molecular dynamics simulation with an implicit solvation model publication-title: Proteins doi: 10.1002/prot.20771 contributor: fullname: Jang – ident: 10.1016/j.bpj.2009.08.046_bib29 – year: 2009 ident: 10.1016/j.bpj.2009.08.046_bib33 contributor: fullname: Delano – volume: 335 start-page: 1029 year: 2004 ident: 10.1016/j.bpj.2009.08.046_bib21 article-title: Temperature dependence of the thermodynamics of helix-coil transition publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2003.11.027 contributor: fullname: Richardson – volume: 100 start-page: 7587 year: 2003 ident: 10.1016/j.bpj.2009.08.046_bib25 article-title: Understanding folding and design: replica-exchange simulations of “Trp-cage” miniproteins publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1330954100 contributor: fullname: Pitera – volume: 383 start-page: 282 year: 2004 ident: 10.1016/j.bpj.2009.08.046_bib14 article-title: Analysis of circular dichroism data publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(04)83012-X contributor: fullname: Greenfield – year: 1993 ident: 10.1016/j.bpj.2009.08.046_bib28 contributor: fullname: Roberts – volume: 307 start-page: 1411 year: 2001 ident: 10.1016/j.bpj.2009.08.046_bib26 article-title: The beta-beta-alpha fold: explorations in sequence space publication-title: J. Mol. Biol. doi: 10.1006/jmbi.2000.4345 contributor: fullname: Sarisky – volume: 121 start-page: 12104 year: 2004 ident: 10.1016/j.bpj.2009.08.046_bib10 article-title: The role of plastic beta-hairpin and weak hydrophobic core in the stability and unfolding of a full sequence design protein publication-title: J. Chem. Phys. doi: 10.1063/1.1822916 contributor: fullname: Lei – volume: 88 start-page: 2854 year: 1991 ident: 10.1016/j.bpj.2009.08.046_bib18 article-title: Calorimetric determination of the enthalpy change for the alpha-helix to coil transition of an alanine peptide in water publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.88.7.2854 contributor: fullname: Scholtz – volume: 291 start-page: 965 year: 1999 ident: 10.1016/j.bpj.2009.08.046_bib19 article-title: A calorimetric study of the folding-unfolding of an alpha-helix with covalently closed N and C-terminal loops publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.3025 contributor: fullname: Taylor – volume: 97 start-page: 3034 year: 2000 ident: 10.1016/j.bpj.2009.08.046_bib27 article-title: De novo protein design: crystallographic characterization of a synthetic peptide containing independent helical and hairpin domains publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.97.7.3034 contributor: fullname: Karle – volume: 34 start-page: 43 year: 2005 ident: 10.1016/j.bpj.2009.08.046_bib1 article-title: How well can simulation predict protein folding kinetics and thermodynamics? publication-title: Annu. Rev. Biophys. Biomol. Struct. doi: 10.1146/annurev.biophys.34.040204.144447 contributor: fullname: Snow – volume: 271 start-page: 342 year: 1996 ident: 10.1016/j.bpj.2009.08.046_bib6 article-title: Design of a monomeric 23-residue polypeptide with defined tertiary structure publication-title: Science doi: 10.1126/science.271.5247.342 contributor: fullname: Struthers – volume: 13 start-page: 501 year: 2000 ident: 10.1016/j.bpj.2009.08.046_bib16 article-title: Thermal unfolding and conformational stability of the recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritima publication-title: Protein Eng. doi: 10.1093/protein/13.7.501 contributor: fullname: Consalvi – volume: 46 start-page: 225 year: 2002 ident: 10.1016/j.bpj.2009.08.046_bib3 article-title: Structure of Met-enkephalin in explicit aqueous solution using replica exchange molecular dynamics publication-title: Proteins doi: 10.1002/prot.1167 contributor: fullname: Sanbonmatsu – volume: 112 start-page: 5938 year: 2008 ident: 10.1016/j.bpj.2009.08.046_bib23 article-title: Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data publication-title: J. Phys. Chem. doi: 10.1021/jp0757715 contributor: fullname: Godoy-Ruiz – volume: 3 start-page: 95 year: 1998 ident: 10.1016/j.bpj.2009.08.046_bib5 article-title: Design and NMR analyses of compact, independently folded ββα motifs publication-title: Fold. Des. doi: 10.1016/S1359-0278(98)00015-7 contributor: fullname: Struthers – volume: 278 start-page: 82 year: 1997 ident: 10.1016/j.bpj.2009.08.046_bib7 article-title: De novo protein design: fully automated sequence selection publication-title: Science doi: 10.1126/science.278.5335.82 contributor: fullname: Dahiyat – volume: 27 start-page: 8063 year: 1988 ident: 10.1016/j.bpj.2009.08.046_bib15 article-title: Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants publication-title: Biochemistry doi: 10.1021/bi00421a014 contributor: fullname: Santoro – volume: 123 start-page: 154105 year: 2005 ident: 10.1016/j.bpj.2009.08.046_bib24 article-title: Convergence of replica exchange molecular dynamics publication-title: J. Chem. Phys. doi: 10.1063/1.2056540 contributor: fullname: Zhang – volume: 130 start-page: 15327 year: 2008 ident: 10.1016/j.bpj.2009.08.046_bib17 article-title: Crystal structure of a ten-amino acid protein publication-title: J. Am. Chem. Soc. doi: 10.1021/ja8030533 contributor: fullname: Honda – volume: 31 start-page: 1463 year: 1991 ident: 10.1016/j.bpj.2009.08.046_bib20 article-title: Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water publication-title: Biopolymers doi: 10.1002/bip.360311304 contributor: fullname: Scholtz – volume: 110 start-page: 22001 year: 2006 ident: 10.1016/j.bpj.2009.08.046_bib9 article-title: Folding transition-state and denatured-state ensembles of FSD-1 from folding and unfolding simulations publication-title: J. Phys. Chem. B doi: 10.1021/jp063716a contributor: fullname: Lei – volume: 259 start-page: 144 year: 1995 ident: 10.1016/j.bpj.2009.08.046_bib22 article-title: Thermal denaturation methods in the study of protein folding publication-title: Methods Enzymol. doi: 10.1016/0076-6879(95)59042-0 contributor: fullname: Freire – year: 2007 ident: 10.1016/j.bpj.2009.08.046_bib32 article-title: TeraGrid: analysis of organization, system architecture, and middleware enabling new types of applications, HPC and grids in action contributor: fullname: Catlett – volume: 13 start-page: 211 year: 1974 ident: 10.1016/j.bpj.2009.08.046_bib30 article-title: Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins publication-title: Biochemistry doi: 10.1021/bi00699a001 contributor: fullname: Chou – volume: 115 start-page: 195 year: 2005 ident: 10.1016/j.bpj.2009.08.046_bib13 article-title: Folding simulations of small proteins publication-title: Biophys. Chem. doi: 10.1016/j.bpc.2004.12.040 contributor: fullname: Kim – volume: 314 start-page: 141 year: 1999 ident: 10.1016/j.bpj.2009.08.046_bib2 article-title: Replica-exchange molecular dynamics method for protein folding publication-title: Chem. Phys. Lett. doi: 10.1016/S0009-2614(99)01123-9 contributor: fullname: Sugita – volume: 354 start-page: 173 year: 2005 ident: 10.1016/j.bpj.2009.08.046_bib4 article-title: Reproducible polypeptide folding and structure prediction using molecular dynamics simulations publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.09.030 contributor: fullname: Seibert – volume: 26 start-page: 1701 year: 2005 ident: 10.1016/j.bpj.2009.08.046_bib31 article-title: GROMACS: fast, flexible, and free publication-title: J. Comput. Chem. doi: 10.1002/jcc.20291 contributor: fullname: Van Der Spoel |
| SSID | ssj0012501 |
| Score | 2.0604846 |
| Snippet | Mini-proteins that contain <50 amino acids often serve as model systems for studying protein folding because their small size makes long timescale simulations... |
| SourceID | pubmedcentral proquest crossref pubmed elsevier |
| SourceType | Open Access Repository Aggregation Database Index Database Publisher |
| StartPage | 2803 |
| SubjectTerms | Amino acids Calorimetry, Differential Scanning Circular Dichroism Computer Simulation Dichroism Differential scanning calorimetry DNA-Binding Proteins - chemistry Folding Hydrogen Bonding Melting Models, Chemical Models, Molecular Molecular dynamics Molecular structure Phase Transition Protein Protein Folding Protein Stability Protein Structure, Secondary Proteins Simulation Stability Temperature Transcription Factors - chemistry Transition Temperature Zinc |
| SummonAdditionalLinks | – databaseName: Open Access: Elsevier Open Archive Journals dbid: ABVKL link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELZKKyQuiHdDaWUkTqimduI4DrftllUFBSEtRb1FseNVXbHZ1W562F_Qv92ZxFm6vA7cosROYnsenzWfZwh5ww2Yfaclq2KrmJQZZ9pJwWxV6YpLgSmekG3xRZ2ey48X6cUWGfZnYZBWGWx_Z9Nbax3uHIXZPJp7j2d8wb0CvucYCUxyfY_sYC5zEO2dwfH3T2frYAJ4-VA4TzHs0Ac3W5qXmV-FrJX6HUcY_Gf39Dv8_JVFecctjR6RhwFP0kH3y4_JlqufkPtdhcnVU3IzoGPc8lb0DNA0LRv62deefcXsDL6mADVbcuzqPe2zk9DZhI7GJ0zQlk1Ah37RUlXpibeXi5lfTg_hsquqAtbhBx3bruwRHZbI5pu6ZrE6pCV8cuynoTjY8hk5H334NjxlofYCs6ClDdMTLq3WiUhSmxqblXHqtEmMcJOJKStrhYG9jjQ2z61B1OLiKpe6FBjX5ACCnpPtela7XUK5AVhguBWq0tIZZZRTpU4dvFYBWlYRedtPeTHvUmwUPffsqoD1wVKZeYHVMiU0lv2iFBtyUoAL-Fe3vX4Bi6CkywLQjgL4y5OIvF4_Be3CkElZu9n1shAKz9omQmQRoX9pkwEQkDEYx4i86CTi5zAAfWdxkkYk25CVdQNM7r35pPaXbZLvOAM3lauX_zfePfKgDXshXzF9RbabxbXbB_TUmIOgHbdZlhjl priority: 102 providerName: Elsevier |
| Title | A Second Look at Mini-Protein Stability: Analysis of FSD-1 Using Circular Dichroism, Differential Scanning Calorimetry, and Simulations |
| URI | https://dx.doi.org/10.1016/j.bpj.2009.08.046 https://www.ncbi.nlm.nih.gov/pubmed/19917235 https://www.proquest.com/docview/215697703 https://search.proquest.com/docview/1671343117 https://search.proquest.com/docview/734142031 https://pubmed.ncbi.nlm.nih.gov/PMC2776296 |
| Volume | 97 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFD5ah5B4QdwJg8pIPKG5jRPHcXnrOqoBG5pUhvoWxY6rZVrSqs0e-gv2t3fsOINxe-AtUpyrz_H5js7n8wG8CxUu-0ZyWkRaUM7TkErDGdVFIYuQM9viybItvoqjM_55nsx3IOn2wjjSvlbloL6sBnV57riVq0oPO57Y8PRkEqXowiMx7EEPw2-XovvSAcZ0L5MnaIzwvytlOlKXWl34HpVygJmhaxmKCUvk1N7-GJd-x52_0id_ikfTR_DQA0kybl_4MeyY-gncb6Ult0_hekxmNtctyDHCaJI35KSsS3pq2zKUNUGM6Vix2w-ka0tClgsynR1SRhyNgEzKteOoksNSn6-X5abax8NWTgWXhUsy063eEZnklsZXmWa93Sc5PnJWVl4VbPMMzqYfv02OqBddoBrds6FyEXItZcziRCdKp3mUGKlixcxiofJCa6YwyeFKj0ZaWbhiomLEZc5sQTNE9PMcdutlbV4CCRXiARVqJgrJjRJKGJHLxOBtBcJkEcD77pdnq7a3RtaRzi4ynCqrkTnKrEwmx8G8m5TMg4M26Ge49v_rsr1uAjPvnZsMYY5A3BvGAby9PYtuZWsleW2WV5uMCbvJNmYsDYD8ZUyKCIBHuCoG8KK1iB-f4a0qgPSOrdwOsF29755BY3fdvb1xv_rvK_fggSt5Wa5i8hp2m_WVeYPIqVF9uDc--P7luA-9T_ODvvObG5pFGqk |
| link.rule.ids | 230,314,727,780,784,885,3506,27569,27924,27925,45663,45874,53791,53793 |
| linkProvider | National Library of Medicine |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFLbGJgQvaNzDuBiJJzQzO3Ech7euoyqsm5C6ob1ZseNqnmhatdlDf8H-9o4Tp1BuD7xFiZ3E9rl81vl8DkLvqAazbyUnZWwE4TyjRFrOiClLWVLOfIonz7Y4FcNz_uUivdhC_e4sjKdVBtvf2vTGWoc7B2E2D-bO-TO-4F4B31MfCUxyeQftABoQIOw7vcNvx6N1MAG8fCicJ4jv0AU3G5qXnl-FrJXyA_Uw-M_u6Xf4-SuL8ie3NNhFDwKexL32lx-iLVs9QnfbCpOrx-imh8d-y1viEaBpXNT4xFWOfPXZGVyFAWo25NjVR9xlJ8GzCR6MjwjDDZsA992ioariI2cuFzO3nO7DZVtVBazDdzw2bdkj3C88m29q68VqHxfwybGbhuJgyyfofPDprD8kofYCMaClNZETyo2UCUtSk2qTFXFqpU40s5OJLkpjmIa9Dtcmz432qMXGZc5lwXxckwIIeoq2q1llnyNMNcACTQ0TpeRWCy2sKGRq4bUC0LKI0PtuytW8TbGhOu7ZlYL18aUyc-WrZXJozLtFURtyosAF_KvbXreAKijpUgHaEQB_aRKht-unoF0-ZFJUdna9VEz4s7YJY1mE8F_aZAAEeAzGMULPWon4MQxA31mcpBHKNmRl3cAn9958UrnLJsl3nIGbysWL_xvvG3RveHYyUqPPp8d76H4TAvPcxfQl2q4X1_YVIKlavw6acguT4BvK |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELagCMQF8SaUh5E4oXo3ThzH4VbtsirQVistlXqz4kfUVE12tZse9hfwtxk7Tml5HbhFip2XZzzfaL7Mh9D7WMG2bwUjJtGcMJbHRFhGiTZGmJhR1-LJsS2O-cEJ-3KanV6T-vKkfa3qUXvRjNr6zHMrV40eDzyx8fxokuTgwgUfr0w1vo3uZCkY2ZCohwICRPYglsdJCknAUND01C61Og-dKsUI8kPfOBTSlsRrvv0xOv2OPn8lUV6LSrOH6EGAk3i_f-xH6JZtH6O7vcDk9gn6vo8XLuM1-BDANC47fFS3NZm75gx1iwFpem7s9iMempPgZYVniymh2JMJ8KRee6Yqntb6bL2sN80eHPaiKrA5XOCF7lWP8KR0ZL7GduvtHi7hlou6Cdpgm6foZPbp2-SABOkFosFJOyKqmGkhUppmOlM6L5PMCpUqaqtKlUZrqiDVYUoXhVYOtNjEFEyU1JU1Y8BAz9BOu2ztC4RjBahAxZpyI5hVXHHLS5FZuCwHsMwj9GH45HLVd9iQA_XsXMJSOaXMQjqxTAaD2bAoMkCEPvRLiAD_mrY7LKAMPrqRAHY4oN84jdC7q7PgXK5iUrZ2ebmRlLtfbVNK8wjhv4zJAQewBPbGCD3vLeLnawSrilB-w1auBrje3jfPgMn7Ht_BxF_-98y36N58OpOHn4-_7qL7vgbmyIvZK7TTrS_ta4BSnXrjneYHGcsceg |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=A+Second+Look+at+Mini-Protein+Stability%3A+Analysis+of+FSD-1+Using+Circular+Dichroism%2C+Differential+Scanning+Calorimetry%2C+and+Simulations&rft.jtitle=Biophysical+journal&rft.au=Feng%2C+Jianwen+A&rft.au=Kao%2C+Jeff&rft.au=Marshall%2C+Garland+R&rft.date=2009-11-15&rft.issn=0006-3495&rft.volume=97&rft.issue=10&rft.spage=2803&rft.epage=2810&rft_id=info:doi/10.1016%2Fj.bpj.2009.08.046&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0006-3495&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0006-3495&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0006-3495&client=summon |