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@ARTICLE{Ma:153350,
author = {Ma, Peixiang and Haller, J. D. and Zajakala, J. and Macek,
P. and Sivertsen, A. C. and Willbold, Dieter and
Boisbouvier, J. and Schanda, P.},
title = {{P}robing transient conformational {S}tates of proteins by
solid-state {R}$_{1ρ}$ relaxation-dispersion {NMR}
spectroscopy},
journal = {Angewandte Chemie / International edition},
volume = {53},
number = {17},
issn = {0570-0833},
address = {Weinheim},
publisher = {Wiley-VCH},
reportid = {FZJ-2014-02982},
pages = {4312-4317},
year = {2014},
abstract = {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.},
cin = {ICS-6},
ddc = {540},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {452 - Structural Biology (POF2-452)},
pid = {G:(DE-HGF)POF2-452},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000334396800004},
pubmed = {pmid:24644028},
doi = {10.1002/anie.201311275},
url = {https://juser.fz-juelich.de/record/153350},
}