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Volume 17, Issue 2-3, Pages 101-126

Structure and Behaviour of Proteins, Nucleic Acids and Viruses from Vibrational Raman Optical Activity

Laurence D. Barron,1 Ewan W. Blanch,1 Iain H. McColl,1 Christoper D. Syme,1 Lutz Hecht,1 and Kurt Nielsen2

1Department of Chemistry, University of Glasgow, Glasgow G12 8QQ, UK
2Department of Chemistry, DTU-207, Technical University of Denmark, DK-2800 Lyngby, Denmark

Copyright © 2003 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


On account of its sensitivity to chirality Raman optical activity (ROA), which may be measured as a small difference in vibrational Raman scattering from chiral molecules in right- and left-circularly polarized incident light, is a powerful probe of structure and behaviour of biomolecules in aqueous solution. Protein ROA spectra provide information on the secondary and tertiary structure of the polypeptide backbone, hydration, side chain conformation and structural elements present in denatured states. Nucleic acid ROA spectra provide information on the sugar ring conformation, the base stacking arrangement and the mutual orientation of the sugar and base rings around the C–N glycosidic link. The ROA spectra of intact viruses provide information on the folds of the coat proteins and the nucleic acid structure. The large number of structure-sensitive bands in protein ROA spectra is especially favourable for fold determination using pattern recognition techniques. This article gives a brief account of the ROA technique and presents the ROA spectra of a selection of proteins, nucleic acids and viruses that illustrate the applications of ROA spectroscopy in biomolecular research.