title: Circular-dichroism and synchrotron-radiation circular-dichroism spectroscopy as tools to monitor protein structure in a lipid environment.
abstract: Circular-dichroism (CD) spectroscopy is a powerful tool for the secondary-structure analysis of proteins. The structural information obtained by CD does not have atomic-level resolution (unlike X-ray crystallography and NMR spectroscopy), but it has the great advantage of being applicable to both nonnative and native proteins in a wide range of solution conditions containing lipids and detergents. The development of synchrotron-radiation CD (SRCD) instruments has greatly expanded the utility of this method by extending the spectra to the vacuum-ultraviolet region below 190 nm and producing information that is unobtainable by conventional CD instruments. Combining SRCD data with bioinformatics provides new insight into the conformational changes of proteins in a membrane environment.
authors: Hiroshima Synchrotron Radiation Center, Hiroshima University, Higashi-Hiroshima, Japan.
authors: Koichi
authors: K
authors: Matsuo
authors: Kunihiko
authors: K
authors: Gekko
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002138:Calibration; D002942:Circular Dichroism / Q000379:methods*; D006801:Humans; D008055:Lipids / Q000737:chemistry*; D008081:Liposomes / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011827:Radiation; D017356:Synchrotrons
chemical_list: D008055:Lipids; D008081:Liposomes; D008565:Membrane Proteins