Resonance Raman Studies of Electron-nuclear Coupling, Time Resolved Dynamics and Magnetic Perturbations of Biomolecules

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The proposed research utilizes resonance Raman and Rayleigh scattering to probe the electronic and nuclear structure/function relationships of biological molecules such as the heme proteins (myoglobin, hemoglobin and cytochrome c). Related techniques, such as electronic absorption and far infrared spectroscopy, are also utilized and theoretical relationship that link a variety of experimental measurements are developed. Further experimental and theoretical studies involving the spectroscopic and kinetic effects of protein conformational distributions are also proposed. Dynamic studies will include the measurement and analysis of ligand binding to heme proteins under a wide variety of sample conditions as well as pump/probe experiments designed to monitor protein folding and conformational relaxation. Laser mediated thermal perturbations will be followed using Stokes/anti-Stokes Raman scattering. Studies of photon induced electron transport kinetics as well as resonance Raman saturation studies are also proposed. Resonance Raman and kinetic studies of biological Single crystals will also be extended. Overall the objectives are to achieve a better understanding of the resonant light scattering properties of biological molecules and to apply this knowledge to the elucidation of their mechanism of action. These studies are significant not only in their relationship to the biological sciences, but also in their connection to the understanding of basic light-matter interactions.