Journal Article

FZJ-2014-02982

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Probing transient conformational States of proteins by solid-state R$_{1ρ}$ relaxation-dispersion NMR spectroscopy

Ma, P.FZJ* ; Haller, J. D. ; Zajakala, J. ; Macek, P. ; Sivertsen, A. C. ; Willbold, D.FZJ* ; Boisbouvier, J. ; Schanda, P. (Corresponding Author)

2014
Wiley-VCH Weinheim

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Please use a persistent id in citations: doi:10.1002/anie.201311275

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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)

Appears in the scientific report 2014

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Database coverage:
; Current Contents - Life Sciences ; Current Contents - Social and Behavioral Sciences ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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