Solution NMR views of dynamical ordering of biomacromolecules

• Published in: Biochimica et biophysica acta Vol. 1862; no. 2; pp. 287 - 306
• Main Authors: Ikeya, Teppei, Ban, David, Lee, Donghan, Ito, Yutaka, Kato, Koichi, Griesinger, Christian
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.02.2018
• Subjects: Dynamical ordering; Dynamics; homeostasis; human diseases; In-cell NMR; Large biomacromolecules; nuclear magnetic resonance spectroscopy; proteins; Solution NMR spectroscopy; Stable isotope labelling; thermodynamics; CPP; R2,0; PRE; SIFT; R1ρ; Rex; TAT; ALS; CHO; MDD; ERNST; IDP; MD; SLO; MF; R2,eff; LBT; R1; R2; ORIUM; ηz; EI; NOE; QME; GAF; RD; RF; GB3; H/D; (C)EST; DEST; Stable isotope labelling; In-cell NMR; PCS; Solution NMR spectroscopy; MFA; PDB; CSA; RDC; Dynamics; SAIL; Dynamical ordering; Large biomacromolecules; CPMG; MBP; SMILE; SRDC2; DIDC; SOD; HPr; NUS; HEK; CS; EROS; TROSY; TRACT; NMR; CCR; MaxEnt; ηxy; HSQC; SLS2
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/j.bbagen.2017.08.020

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.