Side Chain Conformations of Oxytocin and Vasopressin Studied by NMR Observation of Isotopic Isomers1a

David Cowburn, David H. Live, Alan J. Fischman, William C. Agosta

Research output: Contribution to journalArticle

38 Scopus citations

Abstract

The side chain conformations of several residues of oxytocin and [8-arginine]vasopressin are compared by using measurements of the circumjacent vicinal couplings of 1Hα, 13C', and 15N’ to β protons and stereospecific β 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
DOIs
Publication statusPublished - Nov 1983
Externally publishedYes

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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