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

N.P. Cowieson, A.J. Miles, Gautier Robin, Jade Forwood, B. Kobe, J. L. Martin, B. A. Wallace

Research output: Contribution to journalArticlepeer-review

25 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)1142-1146
Number of pages5
JournalProteins: Structure, Function and Genetics
Issue number4
Publication statusPublished - Mar 2008


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