Document Detail


Conformation of somatostatin using scalar coupling constants from 270 and 600 MHz simulated proton magnetic resonance spectra.
MedLine Citation:
PMID:  6132629     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The conformation of the 14 amino acid peptide hormone somatostatin in aqueous solution was investigated through a proton magnetic resonance (PMR) scalar coupling analysis. Experiments were performed at two fields, 270 and 600 MHz, and included double and triple resonance difference scalar decoupling, resolution enhancement and computer simulation. The agreement between simulated and observed spectra at both fields provided support for the correctness of the analysis. The resultant scalar coupling constants, 3J alpha H-NH and 3J alpha B, gave information on the backbone (phi) and side chain (chi 1) torsional angles, respectively, which eliminated either of the proposed conformations of somatostatin as describing a predominant conformer of the molecule in solution under our conditions.
Authors:
L A Buffington; V Garsky; J Rivier; W A Gibbons
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biophysical journal     Volume:  41     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  1983 Mar 
Date Detail:
Created Date:  1983-06-10     Completed Date:  1983-06-10     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  299-304     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Magnetic Resonance Spectroscopy / methods
Protein Conformation
Somatostatin*
Grant Support
ID/Acronym/Agency:
1-F32 AM6089/AM/NIADDK NIH HHS; CM 295.95/CM/NCI NIH HHS; RR 00292/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
51110-01-1/Somatostatin
Comments/Corrections

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