Document Detail

Nmr probes of molecular dynamics: overview and comparison with other techniques.
MedLine Citation:
PMID:  11340055     Owner:  NLM     Status:  MEDLINE    
NMR spin relaxation spectroscopy is a powerful approach for characterizing intramolecular and overall rotational motions in proteins. This review describes experimental methods for measuring laboratory frame spin relaxation rate constants by high-resolution solution-state NMR spectroscopy, together with theoretical approaches for interpreting spin relaxation data in order to quantify protein conformational dynamics on picosecond-nanosecond time scales. Recent applications of these techniques to proteins are surveyed, and investigations of the contribution of conformational chain entropy to protein function are highlighted. Insights into the dynamical properties of proteins obtained from NMR spin relaxation spectroscopy are compared with results derived from other experimental and theoretical techniques.
A G Palmer
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Annual review of biophysics and biomolecular structure     Volume:  30     ISSN:  1056-8700     ISO Abbreviation:  Annu Rev Biophys Biomol Struct     Publication Date:  2001  
Date Detail:
Created Date:  2001-05-07     Completed Date:  2001-08-09     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9211097     Medline TA:  Annu Rev Biophys Biomol Struct     Country:  United States    
Other Details:
Languages:  eng     Pagination:  129-55     Citation Subset:  IM    
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10027, USA.
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MeSH Terms
Biophysics / methods*
Magnetic Resonance Spectroscopy / methods*
Models, Chemical
Models, Theoretical
Time Factors
Grant Support
Reg. No./Substance:

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