Raman study of crystalline peptides containing β turns

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

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

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
Volume211
Issue number2
DOIs
StatePublished - Oct 15 1981

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Amides
Crystalline materials
Peptides
Conformations
Raman scattering
Gramicidin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Raman study of crystalline peptides containing β turns. / Fox, Jay A.; Tu, Anthony T.; Hruby, Victor J; Mosberg, Henry I.

In: Archives of Biochemistry and Biophysics, Vol. 211, No. 2, 15.10.1981, p. 628-631.

Research output: Contribution to journalArticle

Fox, Jay A. ; Tu, Anthony T. ; Hruby, Victor J ; Mosberg, Henry I. / Raman study of crystalline peptides containing β turns. In: Archives of Biochemistry and Biophysics. 1981 ; Vol. 211, No. 2. pp. 628-631.
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