Protein Characterisation by Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy
Circular dichroism (CD) spectroscopy is a well-established technique for the study of proteins. Synchrotron radiation circular dichroism (SRCD) spectroscopy extends the utility of conventional CD spectroscopy (i.e. using laboratory-based instruments) because the 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 presence of strongly absorbing non-chiral components such as salts, buffers, lipids and detergents. This review describes developments in instrumentation, methodologies and bioinformatics that have enabled new applications of the SRCD technique for the study of proteins. It includes examples of the use of SRCD spectroscopy for providing static and dynamic structural information on molecules, including determinations of secondary structures of intact proteins and domains, assessment of protein stability, detection of conformational changes associated with ligand and drug binding, monitoring of environmental effects, examination of the processes of protein folding and membrane insertion, comparisons of mutant and modified proteins, identification of intermolecular interactions and complex formation, determination of the dispositions of proteins in membranes, identification of natively disordered proteins and their binding partners and examination of the carbohydrate components of glycoproteins. It also discusses how SRCD can be used in conjunction with macromolecular crystallography and other biophysical techniques to provide a more complete picture of protein structures and functions, including how proteins interact with other macromolecules and ligands. This review also includes a discussion of potential new applications in structural and functional genomics using SRCD spectroscopy and future instrumentation and bioinformatics developments that will enable such studies. Finally, the appendix describes a number of computational/bioinformatics resources for secondary structure analyses that take advantage of the improved data quality available from SRCD. In summary, this review discusses how SRCD can be used for a wide range of structural and functional studies of proteins.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- DOE - OFFICE OF SCIENCE
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 1019613
- Report Number(s):
- BNL--95458-2011-JA
- Journal Information:
- Quarterly Reviews of Biophysics, Journal Name: Quarterly Reviews of Biophysics Journal Issue: 4 Vol. 42; ISSN QURBAW; ISSN 0033-5835
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
99 GENERAL AND MISCELLANEOUS
BUFFERS
CARBOHYDRATES
CONFORMATIONAL CHANGES
CRYSTALLOGRAPHY
DETECTION
DETERGENTS
DICHROISM
ENVIRONMENTAL EFFECTS
FUNCTIONALS
GLYCOPROTEINS
LIPIDS
MEMBRANES
MONITORING
MUTANTS
PROTEIN STRUCTURE
PROTEINS
SPECTRA
SPECTROSCOPY
STABILITY
SYNCHROTRON RADIATION
SYNCHROTRONS
WAVELENGTHS
national synchrotron light source