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000153350 1001_ $$0P:(DE-Juel1)132033$$aMa, Peixiang$$b0$$ufzj
000153350 245__ $$aProbing transient conformational States of proteins by solid-state R$_{1ρ}$ relaxation-dispersion NMR spectroscopy
000153350 260__ $$aWeinheim$$bWiley-VCH$$c2014
000153350 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1399274436_3046
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000153350 520__ $$aThe function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally accessible conformations are connected, and understanding their structures and relative energies is crucial in rationalizing protein function. Many biomolecular reactions take place within microseconds to milliseconds, and this timescale is therefore of central functional importance. Here we show that R1ρ relaxation dispersion experiments in magic-angle-spinning solid-state NMR spectroscopy make it possible to investigate the thermodynamics and kinetics of such exchange process, and gain insight into structural features of short-lived states.
000153350 536__ $$0G:(DE-HGF)POF2-452$$a452 - Structural Biology (POF2-452)$$cPOF2-452$$fPOF II$$x0
000153350 7001_ $$0P:(DE-HGF)0$$aHaller, J. D.$$b1
000153350 7001_ $$0P:(DE-HGF)0$$aZajakala, J.$$b2
000153350 7001_ $$0P:(DE-HGF)0$$aMacek, P.$$b3
000153350 7001_ $$0P:(DE-HGF)0$$aSivertsen, A. C.$$b4
000153350 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b5
000153350 7001_ $$0P:(DE-HGF)0$$aBoisbouvier, J.$$b6
000153350 7001_ $$0P:(DE-HGF)0$$aSchanda, P.$$b7$$eCorresponding Author
000153350 773__ $$0PERI:(DE-600)2011836-3$$a10.1002/anie.201311275$$n17$$p4312-4317$$tAngewandte Chemie / International edition$$v53$$x0570-0833$$y2014
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000153350 9141_ $$y2014
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