TIME RESOLVED PROTEIN FOLDING USING LAUE WHITE BEAM SMALL ANGLE XRAY SCATTERING

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In addition to exploring "Laue" SAXS, i.e. using very broad-band quasi-white radiation, we have evaluated the use of a narrower broad-band radiation setup using multilayer monochromators. The use of the these multilayers (200 eV bandpass) on BL4-2 resulted in a 20-fold increase of x-ray flux over the normal Si(111) monochromator. This flux increase resulted in better time resolution for time-resolved SAXS protein folding studies. SAXS is the only experimental probe which can give overall size and shape indication of the conformational state of a protein. Time-resolved SAXS studies on the refolding of lysozyme was performed (manuscript in preparation). We have performed preliminary experiments using SAXS to study protein folding initiated with a continuous flow mixer. Control studies show that reasonable radius of gyration measurements can be obtained with this method.