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.
ASJC Scopus subject areas
- Molecular Biology