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Conformational changes by synchrotron radiation circular dichroism spectroscopy

Nature Structural Biology volume 7, pages 708–709 (2000)Cite this article

Circular dichroism (CD) spectroscopy is a valuable technique for detecting conformational changes in proteins as the spectra are sensitive to small alterations in polypeptide backbone structures1. It has been used extensively for both qualitatively and quantitatively examining the binding of ligands to proteins, as well as for deciphering the nature of interactions between proteins and other macromolecules. Using CD spectroscopy, it has been possible to determine the types of secondary structures involved in conformational changes and, in some cases, to quantify the magnitude of the conformational change (number of amino acids involved)2. Some of the advantages of CD as a technique for monitoring conformational changes include the small quantities and low concentrations of protein required, the absence of ‘probe’ molecules, which could distort the results of any measurements made, and the ease and speed at which the experiments can be conducted. Furthermore, the changes can be interpreted on a molecular level in terms of alterations in the polypeptide backbone.

The acquisition of data at lower wavelengths means that the SRCD spectra will be richer, containing more eigenvectors (unique elements) of information than conventional CD spectra due to the additional electronic transitions measured. Consequently, it should be possible to analyze SRCD spectra for a larger number of distinct secondary structural components or folding motifs. Furthermore, as the spectral features in the VUV region for the various types of secondary structures are much more clearly different than they are in the higher wavelength peptide transitions7,9, more accurate secondary structure determinations can be made.

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Figure 1: SRCD (red) and CD (black) spectra of horse myoglobin in aqueous solution.

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Acknowledgements

Supported by a BBSRC Structural Biology Centre Grant to the CPMSD and a beamtime grant from the BBSRC. I thank the CLRC Daresbury Staff, R.W. Janes, and A. Orry for help with data collection and A.C. Willis for the quantitative amino acid analysis.

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  1. Department of Crystallography, Birkbeck College, University of London, London, WC1E 7HX, UK

    B.A. Wallace

  2. Centre for Protein and Membrane Structure and Dynamics, Daresbury Lab, Warrington, WA4 4AD, UK

    B.A. Wallace

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Wallace, B. Conformational changes by synchrotron radiation circular dichroism spectroscopy. Nat Struct Mol Biol 7, 708–709 (2000). https://doi.org/10.1038/78915

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