Comments on the use of a dichromophoric circular dichroism assay for the identification of β‐turns in peptides

J. E. BALDWIN, T. D.W. CLARIDGE, C. HULME, A. RODGER, C. J. SCHOFIELD

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Use of the dichromophoric CD assay for β‐turn formation in peptide sequences has been investigated. The assay involves the observation of Cotton effects in CD spectra, originating from the approach of N‐ and C‐terminal aromatic chromophores in tetrapeptides. The approach of the chromophores was believed to be brought about by a beta;‐turn in the peptide structure. Our investigations were paralleled by NMR studies which revealed the presence of a previously unreported hydrogen bond in the β‐turn conformers, which appears to play a role in the generation of the observed Cotton effects. This suggests caution in the use of the CD technique alone as an assay for β‐turn conformers in peptides.

Original languageEnglish (US)
Pages (from-to)180-183
Number of pages4
JournalInternational journal of peptide and protein research
Volume43
Issue number2
DOIs
StatePublished - Feb 1994
Externally publishedYes

Keywords

  • B‐turn
  • Cotton effect
  • NMR
  • circular dichroism (CD)

ASJC Scopus subject areas

  • Biochemistry

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