Abstract
Synchrotron radiation circular dichroism (SRCD) is a well-established technique in structural biology. The first vacuum-ultraviolet (VUV) to visible (VIS) Diamond Light Source SRCD beamline B23 in UK, is operational since 2009 and available for the user community. B23 has two end-stations, featuring double-grating subtractive monochromators providing unprecedented broad wavelength range from VUV to VIS with low stray light. B23 can be used to investigate the protein secondary structure and tertiary/quaternary structures. A critical assessment of the vacuum UV SRCD spectra previously ascribed to charge transfer and novel protein foldings has revealed instead that the spectral features were due to experimental artifatcs. Major advantages of B23 are production of highly collimated microbeams with photon flux in the vacuum- and far-UV regions several orders of magnitude greater than Xenon light sources of bench-top CD spectropolarimeters. This makes B23 ideal for small sample volumes using capillaries or long pathlength cells (10 cm) for solutions from micromolar to nanomolar. High UV photon flux known to denature/degrade biopolymers can be controlled to become negligible but can also be exploited as novel biopolymer stability and ligand interactions assay. Examples of UV denaturation of proteins and ligand–protein complexes using B23 are described.
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