Shining New Light on Protein Structure and Function thru Synchrotron Radiation Circular Dichroism (SRCD) Spectroscopy

Journal Article · Sat Jan 01 04:00:00 EST 2005 · Aust. Biochem.

OSTI ID:913678

Wallace, B

Circular dichroism (CD) spectroscopy has been employed for more than 50 years for the study of the structure and dynamics of proteins. It is now a workhorse of structural biology, finding applications in the determination of protein secondary structures, monitoring and deciphering protein folding, examining macromolecular interactions, and defining and quantitating protein-ligand binding. For the most part, CD studies have used laboratory-based instruments to measure electronic transitions in the far (190-250 nm), near ultraviolet (UV) (250-300 nm) and visible (> 400 nm) wavelength ranges, which have enabled studies of polypeptide backbones, aromatic amino acids and colored chromophores, respectively. Additional transitions exist at lower wavelengths in the vacuum ultraviolet (VUV) region (<190 nm); however, these transitions tend to be inaccessible to conventional CD instruments, due to the low intensity of their Xenon arc lamp light sources at wavelengths below190 nm. In 1980, the first synchrotron-based CD instruments were constructed, which took advantage of the high photon flux available from synchrotron light sources at these wavelengths. However, the technique of synchrotron radiation circular dichroism (SRCD) did not really take off until enabling studies had been done to show that additional data were obtainable for proteins in the VUV region, that these data were readily accessible with modern beamlines, and most importantly, that new applications of these data existed in structural molecular biology.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 913678
• Report Number(s): BNL--78246-2007-JA
• Journal Information: Aust. Biochem., Journal Name: Aust. Biochem. Vol. 35
• Country of Publication: United States
• Language: English

Related Subjects

43 PARTICLE ACCELERATORS
AMINO ACIDS
AROMATICS
BIOLOGY
DICHROISM
LIGHT SOURCES
MOLECULAR BIOLOGY
MONITORING
PHOTONS
POLYPEPTIDES
PROTEIN STRUCTURE
PROTEINS
SPECTROSCOPY
SYNCHROTRON RADIATION
SYNCHROTRONS
WAVELENGTHS
national synchrotron light source