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Accurate measurement of one-bond H-X heteronuclear dipolar couplings in MAS solid-state NMR.
MedLine Citation:
PMID:  21482161     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
The accurate experimental determination of dipolar-coupling constants for one-bond heteronuclear dipolar couplings in solids is a key for the quantification of the amplitudes of motional processes. Averaging of the dipolar coupling reports on motions on time scales up to the inverse of the coupling constant, in our case tens of microseconds. Combining dipolar-coupling derived order parameters that characterize the amplitudes of the motion with relaxation data leads to a more precise characterization of the dynamical parameters and helps to disentangle the amplitudes and the time scales of the motional processes, which impact relaxation rates in a highly correlated way. Here. we describe and characterize an improved experimental protocol - based on REDOR - to measure these couplings in perdeuterated proteins with a reduced sensitivity to experimental missettings. Because such effects are presently the dominant source of systematic errors in experimental dipolar-coupling measurements, these compensated experiments should help to significantly improve the precision of such data. A detailed comparison with other commonly used pulse sequences (T-MREV, phase-inverted CP, R18(2)(5), and R18(1)(7)) is provided.
Authors:
Paul Schanda; Beat H Meier; Matthias Ernst
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-3-21
Journal Detail:
Title:  Journal of magnetic resonance (San Diego, Calif. : 1997)     Volume:  -     ISSN:  1096-0856     ISO Abbreviation:  -     Publication Date:  2011 Mar 
Date Detail:
Created Date:  2011-4-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9707935     Medline TA:  J Magn Reson     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
Copyright © 2011 Elsevier Inc. All rights reserved.
Affiliation:
Physical Chemistry, ETH Zürich, Wolfgang-Pauli-Strasse 10, 8093 Zürich, Switzerland; Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA, Univ. Grenoble 1, 41, rue Jules Horowitz, F-38027 Grenoble Cedex, France.
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