This title appears in the Scientific Report : 2014 

Probing transient conformational States of proteins by solid-state R$_{1ρ}$ relaxation-dispersion NMR spectroscopy
Ma, Peixiang
Haller, J. D. / Zajakala, J. / Macek, P. / Sivertsen, A. C. / Willbold, Dieter / Boisbouvier, J. / Schanda, P. (Corresponding Author)
Strukturbiochemie ; ICS-6
Angewandte Chemie / International edition, 53 (2014) 17, S. 4312-4317
Weinheim Wiley-VCH 2014
10.1002/anie.201311275
24644028
Journal Article
Structural Biology
Please use the identifier: http://dx.doi.org/10.1002/anie.201311275 in citations.
The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally accessible conformations are connected, and understanding their structures and relative energies is crucial in rationalizing protein function. Many biomolecular reactions take place within microseconds to milliseconds, and this timescale is therefore of central functional importance. Here we show that R1ρ relaxation dispersion experiments in magic-angle-spinning solid-state NMR spectroscopy make it possible to investigate the thermodynamics and kinetics of such exchange process, and gain insight into structural features of short-lived states.