Synchrotron radiation circular dichroism (SRCD) spectroscopy: an enhanced method for examining protein conformations and protein interactions. (26th July 2010)

• Record Type: Journal Article
• Authors: Wallace, B.A.; Janes, Robert W.
• Is Part Of: Biochemical Society transactions. Volume 38:Number 4(2010)
• Page Start: 861
• Page End: 873
• Publication Date: 2010-07-26
• Subjects: circular dichroism spectroscopy (CD spectroscopy) -- macromolecular complex -- protein characterization -- Protein Circular Dichroism Data Bank (PCDDB) -- spectroscopic method -- synchrotron radiation circular dichroism spectroscopy (SRCD spectroscopy); Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0380861
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : CD (circular dichroism) spectroscopy is a well-established technique in structural biology. SRCD (synchrotron radiation circular dichroism) spectroscopy extends the utility and applications of conventional CD spectroscopy (using laboratory-based instruments) because the high flux of a synchrotron enables collection of data at lower wavelengths (resulting in higher information content), detection of spectra with higher signal-to-noise levels and measurements in the presence of absorbing components (buffers, salts, lipids and detergents). SRCD spectroscopy can provide important static and dynamic structural information on proteins in solution, including secondary structures of intact proteins and their domains, protein stability, the differences between wild-type and mutant proteins, the identification of natively disordered regions in proteins, and the dynamic processes of protein folding and membrane insertion and the kinetics of enzyme reactions. It has also been used to effectively study protein interactions, including protein–protein complex formation involving either induced-fit or rigid-body mechanisms, and protein–lipid complexes. A new web-based bioinformatics resource, the Protein Circular Dichroism Data Bank (PCDDB), has been created which enables archiving, access and analyses of CD and SRCD spectra and supporting metadata, now making this information publicly available. To summarize, the developing method of SRCD spectroscopy has the potential for playing an important role in new types of studies of protein conformations and their complexes.