Comments on the use of a dichromophoric circular dichroism assay for the identification of beta-turns in peptides.

Journal article

Use of the dichromophoric CD assay for beta-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 beta-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 beta-turn conformers in peptides.

Authors: Baldwin, J; Claridge, T; Hulme, C; Rodger, A; Schofield, C

• Publication status: Published
• Journal: International journal of peptide and protein research
• Volume: 43
• Issue: 2
• Pages: 180-183
• Publication date: 1994-02-01
• ISSN: 0367-8377
• Language: English
• Keywords: Peptides; Protein Structure, Secondary; Magnetic Resonance Spectroscopy; Amino Acid Sequence; Circular Dichroism; Hydrogen Bonding; Molecular Sequence Data