Protein Function and Dynamics

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This research project is designed to a) further characterize the internal dynamics of selected proteins, b) focus on the effects of viscosity, pressure and temperature on the dynamics and function of proteins and c) develop fluorescence acquisition and analysis protocols for a more realistic and accurate relationship between physical models and experimental data. Dr. Eftink will use the methods of multi-frequency phase/modulation fluorometry and solute fluorescence quenching reactions to characterize the emission of individual tryptophan residues in selected proteins. The dynamic properties of proteins are a matter of fundamental importance in the understanding of ligand binding, catalysis, cooperative effects, protein-protein recognition and other functional aspects of proteins. It is clear that there is an important need to know more than the static three-dimensional structure of proteins in order to unravel the mysteries of their function. Molecular-dynamics calculations can provide insightful simulations of possible events, but these calculations must always be guided and/or supported by empirical experimental measures of protein dynamics. Solute quenching and other fluorescence techniques have contributed greatly to the present data base regarding the fluctuations in proteins on the nanosecond time scale. Further development of these fluorescence techniques should enhance the ability to relate photophysical kinetic models to fluorescence data.***//