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    Evaluating protein : protein complex formation using synchrotron radiation circular dichroism spectroscopy

    Cowieson, N.P. and Miles, Andrew J. and Robin, G. and Forwood, J.K. and Kobe, B. and Martin, J.L. and Wallace, Bonnie A. (2008) Evaluating protein : protein complex formation using synchrotron radiation circular dichroism spectroscopy. Proteins-Structure, Function and Bioinformatics 70 (2), pp. 1142-1146. ISSN 0887-3585.

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    Abstract

    Circular dichroism (CD) spectroscopy beamlines at synchrotrons produce dramatically higher light flux than conventional CD instruments. This property of synchrotron radiation circular dichroism (SRCD) results in improved signal-to-noise ratios and allows data collection to lower wavelengths, characteristics that have led to the development of novel SRCD applications. Here we describe the use of SRCD to study protein complex formation, specifically evaluating the complex formed between carboxypeptidase A and its protein inhibitor latexin. Crystal structure analyses of this complex and the individual proteins reveal only minor changes in secondary structure of either protein upon complex formation (i.e., it involves only rigid body interactions). Conventional CD spectroscopy reports on changes in secondary structure and would therefore not be expected to be sensitive to such interactions. However, in this study we have shown that SRCD can identify differences in the vacuum ultraviolet CD spectra that are significant and attributable to complex formation. Proteins 2008. © 2007 Wiley-Liss, Inc.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): synchrotron radiation circular dichroism spectroscopy, latexin, carboxypeptidase A, protein–protein interactions, secondary structure, complex formation, new methods
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Bioinformatics, Bloomsbury Centre for, Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 04 Aug 2010 14:09
    Last Modified: 07 Dec 2016 15:05
    URI: http://eprints.bbk.ac.uk/id/eprint/1187

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