Conformation of oxytocin studied by laser Raman spectroscopy

Anthony T. Tu, Jón B. Bjarnason, Victor J. Hruby

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Abstract

The peptide backbone conformation and salient structural details of oxytocin were examined by laser Raman spectroscopy. Spectra were obtained in the solid phase, water, 2H2O, and dimethyl sulfoxide solutions. A distinct Amide I band was obtained at 1663 cm-1 for aqueous and deuterated samples and 1666 cm-1 for the solid sample. A relatively high frequency Amide III band at 1260 cm-1 was obtained. It is concluded that these Amide I and III bands arise from the "β-turn"-like conformation of oxytocin. The tyrosine side chain, according to the I850 cm-1/I830cm-1 intensity ratio, is exposed to the solvent. The S-S stretching vibration at 512 cm-1 indicates the conformation of C-C-S-S-C-C in the disulfide bridge of oxytocin in the ring is gauche-gauche-gauche.

Original languageEnglish (US)
Pages (from-to)530-533
Number of pages4
JournalBBA - Protein Structure
Volume533
Issue number2
DOIs
StatePublished - Apr 26 1978

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ASJC Scopus subject areas

  • Medicine(all)

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