Structural characterization of proteins and viruses using Raman optical activity

被引:43
|
作者
Blanch, EW
McColl, IH
Hecht, L
Nielsen, K
Barron, LD
机构
[1] UMIST, Dept Biomol Sci, Manchester M60 1QD, Lancs, England
[2] Univ Glasgow, Dept Chem, Glasgow G12 8QQ, Lanark, Scotland
[3] Tech Univ Denmark, Dept Chem, DTU 207, DK-2800 Lyngby, Denmark
关键词
Raman optical activity; chirality; protein conformation; fold recognition; virus structure;
D O I
10.1016/j.vibspec.2003.12.005
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
The sensitivity to chirality of Raman optical activity (ROA), which we measure as a small difference in vibrational Raman scattering from chiral molecules in right- and left-circularly polarized incident light, makes it a powerful probe of the structure and behaviour of biomolecules in aqueous solution. Protein ROA spectra provide information on the secondary and tertiary structure of the polypeptide backbone and effects of the local environment, including hydration and the side chain conformations of particular residues. The large number of structure-sensitive bands in protein ROA spectra is especially favourable for fold determination using pattern recognition techniques. Intact viruses may also be studied and their ROA spectra provide information not only on the folds of the coat proteins but also about the conformation of the encapsidated nucleic acid. In this article we present the ROA spectra of several proteins and viruses in order to illustrate some of the applications of ROA spectroscopy in biomolecular research. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:87 / 92
页数:6
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