Dynamics of proteins and amorphous solids and transport phenomena in proteins.

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Proteins perform a broad variety of tasks in living organisms, including catalysis, transport of electrons, ions and small molecules, conversion and storage of energy, signal transduction, etc. The manifold of possible conformational states of a protein can be described using the concept of the energy landscape. Information on distributions of barriers on the protein energy landscapes is necessary to better understand conformational changes and folding. This information can be obtained by methods of high-resolution optical spectroscopy, among others, as pigment molecules embedded into protein serve as very sensitive probes to structural properties and dynamics of their environment. We also seek to determine the molecular nature of the entities involved in the conformational changes observed in optical experiments. Since we utilize proteins involved in the processes of photosynthesis as model systems, the results also have potential implications for the renewable energy field. They answer the question of how surrounding protein affects light-harvesting by pigment networks and makes it most effective. We also seek insight into heat dissipation in proteins on atomic level and developing reliable protocols for measuring the effective local temperature in proteins, particularly under illumination. Our studies will be further expanded to spectroscopy of pigment-protein complexes with various degrees of confinement and deformation using convex lens induced confinement method. Subsequent developments of this method will include confining pigment-protein complexes between conducting surfaces for reduction or oxidation of cofactors for spectroscopy measurements, mediator-less photocurrent generation by photosynthetic reaction centers for sensors applications, as well as exploration of confined water.