Observing biological dynamics at atomic resolution using NMR

被引:248
作者
Mittermaier, Anthony K. [1 ]
Kay, Lewis E. [2 ,3 ]
机构
[1] McGill Univ, Dept Chem, Montreal, PQ H3A 2K6, Canada
[2] Univ Toronto, Dept Chem, Toronto, ON M5S 1A8, Canada
[3] Univ Toronto, Dept Biochem & Mol Genet, Toronto, ON M5S 1A8, Canada
基金
加拿大健康研究院;
关键词
NUCLEAR-MAGNETIC-RESONANCE; RESIDUAL DIPOLAR COUPLINGS; MOLECULAR-WEIGHT PROTEINS; RELAXATION DISPERSION NMR; TIME-SCALE DYNAMICS; MODEL-FREE APPROACH; CHARACTERIZING CHEMICAL-EXCHANGE; MALTODEXTRIN-BINDING-PROTEIN; ORDER PARAMETERS; CONFORMATIONAL ENTROPY;
D O I
10.1016/j.tibs.2009.07.004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Biological macromolecules are highly flexible and continually undergo conformational fluctuations on a broad spectrum of timescales. It has long been recognized that dynamics have an important role in the action of these molecules. However, the relationship between molecular function and motion is extremely challenging to delineate, because the conformational space available to macromolecules is vast and the relevant excursions can be infrequent and short-lived. Recent advances in solution nuclear magnetic resonance (NMR) spectroscopy permit biomolecular dynamics to be observed with unprecedented detail. Applications of these new NMR techniques to the study of fundamental processes such as binding and catalysis have provided new insights into how living systems operate at an atomic level.
引用
收藏
页码:601 / 611
页数:11
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