β-sheet and associated turn signatures in vibrational Raman optical activity spectra of proteins

Wen, Z.Q., Hecht, L. and Barron, L.D. (1994) β-sheet and associated turn signatures in vibrational Raman optical activity spectra of proteins. Protein Science, 3(3), pp. 435-439. (doi: 10.1002/pro.5560030308) (PMID:7912598) (PMCID:PMC2142703)

Abstract

We have measured the aqueous solution vibrational Raman optical activity (ROA) spectra of concanavalin A, α-chymotrypsin, and β-lactoglobulin, all of which are rich in β-sheet, together with that of the model β-turn peptide L-pro-L-leu-gly-NH2. Possible ROA signatures of antiparallel β-sheet include a strong sharp positive band at ∼ 1,313 cm” associated with backbone amide III CαH and NH deformations, and an amide I couplet, negative at low wavenumber and positive at high, centered at ∼1,658 cm−1. Negative ROA bands in the range ∼1,340-1,380 cm−1, which might originate in glycine CH2 deformations, appear to be characteristic of β-turns. Our results provide further evidence that ROA is a more incisive probe of protein conformation than conventional vibrational spectroscopy, infrared, or Raman, because only those few vibrational coordinates within a given normal mode that sample the skeletal chirality directly contribute to the corresponding ROA band intensity.

• Item Type: Articles
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Hecht, Dr Lutz and Barron, Professor Laurence
• Authors: Wen, Z.Q., Hecht, L., and Barron, L.D.
• College/School: College of Science and Engineering > School of Chemistry
• Journal Name: Protein Science
• Publisher: Cambridge University Press
• ISSN: 0961-8368
• ISSN (Online): 1469-896X