Synchrotron radiation circular dichroism spectroscopy information
Synchrotron Radiation Circular Dichroism
Synchrotron radiation circular dichroism spectroscopy, commonly referred to as SRCD and also known as VUV-circular dichroism or VUVCD spectroscopy, is a powerful extension to the technique of circular dichroism (CD) spectroscopy, often used to study structural properties of biological molecules such as proteins and nucleic acids. The physical principles of SRCD are essentially identical to those of CD, in that the technique measures the difference in absorption (ΔA) of left (AL) and right (AR) circularly polarized light (ΔA=AL-AR) by a sample in solution. To obtain a CD(SRCD) spectrum the sample must be innately optically active (chiral), or, in some way be induced to have chiral properties, as only then will there be an observable difference in absorption of the left and right circularly polarized light. The major advantages of SRCD over CD arise from the ability to measure data over an extended wavelength range into the vacuum ultra violet (VUV) end of the spectrum. As these measurements are utilizing a light source with a higher photon flux (quantity of light stricking a given surface area) than a bench-top CD machine it means data are more accurate at these extended wavelengths because there is a larger signal over the background noise (the signal-to-noise ratio) and, generally, less sample is needed when recording the spectra and there is more information content available in the data.[1] Many beamlines now exist around the world to enable the measurement of SRCD data.
^Wallace, B. A. (2000). "Synchrotron radiation circular-dichroism spectroscopy as a tool for investigating protein structures". Journal of Synchrotron Radiation. 7 (5). International Union of Crystallography (IUCr): 289–295. doi:10.1107/s0909049500009262. ISSN 0909-0495. PMID 16609210.
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