Franklyn G. Prendergast, M.D., Ph.D.

Proteins are now known to exhibit thermally driven structural fluctuations. These dynamic events are apparently important for protein function. In our lab, laser-based fluorescence and NMR spectroscopic techniques are used to probe protein dynamics on the picosecond to nanosecond time scale. The experimental data are compared to mathematical simulations of protein structure and dynamics, and computer molecular graphics are used to provide visual displays of bench experimental and simulated results. Although a broad variety of proteins are employed in these studies, we have a particular interest in the biochemistry and pharmacology of vital intracellular, Ca++-dependent proteins such as calmodulin and troponin-C (TnC). Calmodulin, in the presence of Ca++, binds to and regulates the function of several important intracellular enzymes and therefore is a key intermediate in the Ca++ mediated regulation of cellular events. Ca++ binding to TnC regulates muscle contraction. Optical spectroscopic, NMR, and calorimetric techniques are being used to determine the structural and dynamic factors which mediate Ca++ and Mg++ regulation of these proteins' functions.

Research interests

• Structure, dynamics and function of proteins.
• Biochemistry and biophysics of bioluminescence.
• Bioimaging.