SMALL ANGLE X-RAY SCATTERING AND HYDRATION FORCES IN PROTEIN FOLDING

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The experimental repertoire of protein structure determination is highly developed, and is typical of research conducted at the various protein crystallography beam lines around the world. Even though it is well appreciated that water environment is a vital determinant of protein tertiary structure, the experimental tools available to characterize aqueous environment in terms of structure and forces are comparatively minimal at present. We have combined our expertise in wide-angle solution scattering experiments, simulations, and theory, to define a model systems approach to determine hydration structure and forces in both early and late stages of protein folding. The aim of this proposal is to extend our wide-angle experiments on these simplified model systems to small angle x-ray scattering, to study the role of the hydrophobic effect and the hydration water. These new experiments, requiring an high flux spectrometer that cover Q < 0.4 A-1, will allow us to address an important biophysical question as to the role of hydration forces in protein folding.