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

Cowieson, Nathan P., Miles, Andrew J., Robin, Gautier, Forwood, Jade K., Kobe, Bostjan, Martin, Jennifer L. and Wallace, B. A. (2008) Evaluating protein: Protein complex formation using synchrotron radiation circular dichroism spectroscopy. Proteins: Structure Function Bioinformatics, 70 4: 1142-1146. doi:10.1002/prot.21631


Author Cowieson, Nathan P.
Miles, Andrew J.
Robin, Gautier
Forwood, Jade K.
Kobe, Bostjan
Martin, Jennifer L.
Wallace, B. A.
Title Evaluating protein: Protein complex formation using synchrotron radiation circular dichroism spectroscopy
Journal name Proteins: Structure Function Bioinformatics   Check publisher's open access policy
ISSN 0887-3585
Publication date 2008-03-01
Year available 2007
Sub-type Article (original research)
DOI 10.1002/prot.21631
Volume 70
Issue 4
Start page 1142
End page 1146
Total pages 4
Place of publication USA
Publisher Wiley-liss, Div John Wiley and Sons
Language eng
Subject C1
270199 Biochemistry and Cell Biology not elsewhere classified
780105 Biological sciences
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. 2007 Wiley-Liss, Inc.
Keyword Synchrotron radiation circular dichroism spectroscopy
Latexin
Carboxypeptidase A
protein-protein interactions
secondary structure
complex formation
new methods
Q-Index Code C1
Q-Index Status Confirmed Code
Additional Notes Published Online: 25 Sep 2007

 
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Created: Tue, 22 Apr 2008, 19:20:29 EST by Cody Mudgway on behalf of Institute for Molecular Bioscience