Observing biological dynamics at atomic resolution using NMR.
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.
Department of Chemistry, McGill University, 801 Sherbrooke St. W., #322, Montreal, Quebec, Canada, H3A 2K6. anthony.mittermaier@mcgill.ca
Anthony K
AK
Mittermaier
Lewis E
LE
Kay
D049071:Endopeptidase Clp / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D013816:Thermodynamics
D049071:Endopeptidase Clp