Circular Dichroism: Studies of Proteins

Kelly, S.M. and Price, N.C. (2009) Circular Dichroism: Studies of Proteins. In: Encyclopedia of Life Sciences. Wiley. (doi:10.1002/9780470015902.a0003043.pub2)

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Publisher's URL: http://onlinelibrary.wiley.com/doi/10.1002/9780470015902.a0003043.pub2/full

Abstract

Circular dichroism (CD) is the differential absorption of the left- and right-circularly polarized components of plane-polarized electromagnetic radiation. It can provide structural and dynamic information about biological macromolecules, particularly proteins. The CD spectra in the far-UV (typically 180-240 nm) can give reliable quantitative estimates of the proportions of secondary structural features (helix, sheet, turn, etc.) present in proteins. The spectra in the near-UV (260-320 nm) can be used to explore the environments of aromatic amino acid side-chains and hence to give a measure of tertiary structure. Although CD cannot provide the high-resolution structural data available from X-ray crystallography or nuclear magnetic resonance, its convenience and applicability under a wide variety of experimental conditions make it the technique of choice in many applications, including exploring protein-ligand interactions, conformational changes and protein folding.

Item Type:Book Sections
Status:Published
Glasgow Author(s) Enlighten ID:Price, Prof Nicholas and Kelly, Dr Sharon
Authors: Kelly, S.M., and Price, N.C.
College/School:College of Medical Veterinary and Life Sciences
Publisher:Wiley

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