Document Detail


Conformation of cyclolinopeptide a observed by nuclear magnetic resonance spectroscopy.
MedLine Citation:
PMID:  16591928     Owner:  NLM     Status:  PubMed-not-MEDLINE    
Abstract/OtherAbstract:
The 220 MHz spectrum of the cyclic nonapeptide Phe-Phe-Leu-Ile-Ile-Leu-Val-Pro-Pro (all L), designated cyclolinopeptide A, is analyzed by decoupling, exchange of peptide NH protons with deuterium, and measurement of the temperature dependence of the NH chemical shift. Measurement of the NH doublet spacings gives values of J(Nalpha), the vicinal coupling of alpha-CH and NH protons of specific amino acid residues. These in turn provide estimates of the rotation angles [unk] about the HN-C(alpha)H(alpha) bonds, which in combination with energy minimization studies, allow the determination of the conformation of the main chain. It is concluded that this polypeptide in dimethylsulfoxide solution does not contain intramolecular hydrogen bonds. Deuterium-exchange rates and temperature-dependence studies indicate that of the seven peptide NH protons, five are exposed to solvent, while two, which exchange somewhat more slowly than the others, may be situated in the interior of the ring.
Authors:
A I Brewster; F A Bovey
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  68     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1971 Jun 
Date Detail:
Created Date:  2010-06-29     Completed Date:  2010-06-29     Revised Date:  2010-09-15    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1199-202     Citation Subset:  -    
Affiliation:
Bell Telephone Laboratories, Incorporated, Murray Hill, New Jersey 07974.
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