Raman study of crystalline peptides containing β turns

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

doi:10.1016/0003-9861(81)90498-7

Raman study of crystalline peptides containing β turns

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

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27 Scopus citations

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 language	English (US)
Pages (from-to)	628-631
Number of pages	4
Journal	Archives of Biochemistry and Biophysics
Volume	211
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(81)90498-7
State	Published - Oct 15 1981
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/0003-9861(81)90498-7

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@article{beef5d1e5add4e82924c803ddb368139,

title = "Raman study of crystalline peptides containing β turns",

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.",

author = "Fox, {Jay A.} and Tu, {Anthony T.} and Hruby, {Victor J.} and Mosberg, {Henry I.}",

note = "Funding Information: 1 This work was supported in part, by USPHS Grant AM 17420 to V.J.H. and 5 ROl GM 19172 to A.T.T. {\textquoteright} To whom correspondence should be addressed.",

year = "1981",

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doi = "10.1016/0003-9861(81)90498-7",

language = "English (US)",

volume = "211",

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TY - JOUR

T1 - Raman study of crystalline peptides containing β turns

AU - Fox, Jay A.

AU - Tu, Anthony T.

AU - Hruby, Victor J.

AU - Mosberg, Henry I.

N1 - Funding Information: 1 This work was supported in part, by USPHS Grant AM 17420 to V.J.H. and 5 ROl GM 19172 to A.T.T. ’ To whom correspondence should be addressed.

PY - 1981/10/15

Y1 - 1981/10/15

N2 - 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.

AB - 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.

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JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

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ER -

Raman study of crystalline peptides containing β turns

Abstract

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