New tools provide new insights in NMR studies of protein dynamics.
There is growing evidence that structural flexibility plays a central role in the function of protein molecules. Many of the experimental data come from nuclear magnetic resonance (NMR) spectroscopy, a technique that allows internal motions to be probed with exquisite time and spatial resolution. Recent methodological advancements in NMR have extended our ability to characterize protein dynamics and promise to shed new light on the mechanisms by which these molecules function. Here, we present a brief overview of some of the new methods, together with applications that illustrate the level of detail at which protein motions can now be observed.
Mittermaier
Anthony
A
Department of Chemistry, McGill University, Montreal, Quebec H3A 2K6, Canada. anthony.mittermaier@mcgill.ca.
Kay
Lewis E
LE
D001426:Bacterial Proteins / Q000737:chemistry; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D007700:Kinetics; D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D051076:Proto-Oncogene Proteins c-fyn / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics; D018909:src Homology Domains
D001426:Bacterial Proteins; C034284:IgG Fc-binding protein, Streptococcus; D011506:Proteins; D051076:Proto-Oncogene Proteins c-fyn