Conformation of oxytocin studied by laser Raman spectroscopy

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

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


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
Issue number2
StatePublished - Apr 26 1978

ASJC Scopus subject areas

  • General Medicine


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