TY  - JOUR
AU  - Ma, Peixiang
AU  - Haller, J. D.
AU  - Zajakala, J.
AU  - Macek, P.
AU  - Sivertsen, A. C.
AU  - Willbold, Dieter
AU  - Boisbouvier, J.
AU  - Schanda, P.
TI  - Probing transient conformational States of proteins by solid-state R$_{1ρ}$ relaxation-dispersion NMR spectroscopy
JO  - Angewandte Chemie / International edition
VL  - 53
IS  - 17
SN  - 0570-0833
CY  - Weinheim
PB  - Wiley-VCH
M1  - FZJ-2014-02982
SP  - 4312-4317
PY  - 2014
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000334396800004
C6  - pmid:24644028
DO  - DOI:10.1002/anie.201311275
UR  - https://juser.fz-juelich.de/record/153350
ER  -