Abstract :
Circular dichroism (CD) spectroscopy is a well-established technique for thestudy of proteins. Synchrotron radiation circular dichroism (SRCD) spectroscopy extends theutility of conventional CD spectroscopy (i.e. using laboratory-based instruments) becausethe high light flux from a synchrotron enables collection of data to lower wavelengths,detection of spectra with higher signal-to-noise levels and measurements in the presenceof strongly absorbing non-chiral components such as salts, buffers, lipids and detergents.This review describes developments in instrumentation, methodologies and bioinformatics thathave enabled new applications of the SRCD technique for the study of proteins. It includesexamples of the use of SRCD spectroscopy for providing static and dynamic structuralinformation on molecules, including determinations of secondary structures of intact proteinsand domains, assessment of protein stability, detection of conformational changes associatedwith ligand and drug binding, monitoring of environmental effects, examination of theprocesses of protein folding and membrane insertion, comparisons of mutant and modifiedproteins, identification of intermolecular interactions and complex formation, determinationof the dispositions of proteins in membranes, identification of natively disordered proteins and their binding partners and examination of the carbohydrate components of glycoproteins. Italso discusses how SRCD can be used in conjunction with macromolecular crystallography andother biophysical techniques to provide a more complete picture of protein structures andfunctions, including how proteins interact with other macromolecules and ligands. This reviewalso includes a discussion of potential new applications in structural and functional genomicsusing SRCD spectroscopy and future instrumentation and bioinformatics developments thatwill enable such studies. Finally, the appendix describes a number of computational/bioinformatics resources for secondary structure analyses that take advantage of the improveddata quality available from SRCD. In summary, this review discusses how SRCD can be usedfor a wide range of structural and functional studies of proteins
