Document Detail

Nuclear magnetic relaxation dispersion study of the dynamics in solid homopolypeptides.
MedLine Citation:
PMID:  17345629     Owner:  NLM     Status:  MEDLINE    
The (1)H nuclear magnetic relaxation dispersion profiles were measured from 10 kHz to 30 MHz as a function of temperature for polyglycine, polyalanine, polyvaline, and polyphenylalanine to examine the contributions of different side chain motions to the polypeptide proton relaxation rate constants. The spin-fracton theory for (1)H relaxation is modified to account for high frequency motions of side chains that are dynamically connected to the linear polymer backbone. The (1)H relaxation is dominated by propagation of rare disturbances along the backbone of the polymer. The side-chain dynamics cause an off-set in the field dependence of the (1)H spin-lattice relaxation rate constants which obey a power law in the Larmor frequency in the limit of low and high magnetic field strength.
Yanina Goddard; Jean-Pierre Korb; Robert G Bryant
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biopolymers     Volume:  86     ISSN:  0006-3525     ISO Abbreviation:  Biopolymers     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-04-30     Completed Date:  2007-07-18     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372525     Medline TA:  Biopolymers     Country:  United States    
Other Details:
Languages:  eng     Pagination:  148-54     Citation Subset:  IM    
Copyright Information:
Copyright 2007 Wiley Periodicals, Inc.
Chemistry Department, University of Virginia Charlottesville, VA 22904, USA.
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MeSH Terms
Magnetic Resonance Spectroscopy*
Peptides / chemistry*
Protein Conformation
Reg. No./Substance:
0/Peptides; 25191-17-7/polyalanine; 25609-85-2/polyvaline; 25718-94-9/polyglycine; 30394-07-1/polyphenylalanine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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