Side chain conformations of oxytoxin and vasopressin studied by NMR observation of isotopic isomers

David Cowburn, D. H. Live, A. J. Fischman, W. C. Agosta

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

The side chain conformations of several residues of oxytocin and left bracket 8-arginine right bracket vasopressin are compared by using measurements of the circumjacent vicinal couplings of **1H** alpha , **1**3C prime , and **1**5N prime to beta protons and stereospecific beta deuteration in series of 18 specifically designed and synthesized isotopic isomers. The conformation(s) of half-cystyls-1 and -6 and tyrosyl-2 is (are) markedly similar when comparing the two peptides, and other residues show only small differences. conformational classes of side chain are identified. It is concluded that most of the side chain conformations are largely uninfluenced by the differences in the primary structures of the two peptides.

Original languageEnglish (US)
Pages (from-to)7435-7442
Number of pages8
JournalJournal of the American Chemical Society
Volume105
Issue number25
StatePublished - Jan 1 1983
Externally publishedYes

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Vasopressins
Isomers
Conformations
Nuclear magnetic resonance
Observation
Peptides
Oxytocin
Arginine
Protons

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Side chain conformations of oxytoxin and vasopressin studied by NMR observation of isotopic isomers. / Cowburn, David; Live, D. H.; Fischman, A. J.; Agosta, W. C.

In: Journal of the American Chemical Society, Vol. 105, No. 25, 01.01.1983, p. 7435-7442.

Research output: Contribution to journalArticle

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