Abstract
Recent biological optical spectroscopic studies have correlated discrete spectroscopic states with biological function in several systems. One of the challenges of molecular biophysics is to correlate structural changes with these spectroscopic states. From small-angle x-ray scattering one can obtain a key structural parameter, the radius of gyration of solubilized proteins. The method described in this paper would permit determination small changes in the radius using polychromatic synchrotron radiation. The high flux of the storage ring combined with an enhancement factor of approximately 10(4), obtained by removing the requirement for monochromatic radiation, will permit determining the radius on a millisecond time scale. Unlike energy-dispersive methods, this method would use all available energies over a wide range of angles.
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Selected References
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