Raman study of crystalline peptides containing β turns

Jay A. Fox, Anthony T. Tu, Victor J. Hruby, Henry I. Mosberg

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


The Raman spectra of crystalline H-ProLeuGlyNH2 which has a type II β turn, crystalline S-benzylCysProLeuGlyNH2 which has a type I β-turn, and crystalline gramicidin S which has two β turns and β-sheet structure in its conformation, were investigated. The amide I and amide III bands of the peptides with β turns were generally different from those which are diagnostic for α-helix and β-sheet conformations. The patterns of the amide I and amide III bands, when examined together, indicate that Raman spectra can provide diagnostic evidence for β-turn structure in peptides.

Original languageEnglish (US)
Pages (from-to)628-631
Number of pages4
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Oct 15 1981
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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