My scientific interest is in understanding life on the atomic and molecular levels. Understanding the processes underlying protein folding and stability, recognition, and catalysis requires knowledge of the atomic details of protein structure and dynamics. In order to comprehend the complex protein machinery, we have to know how various parts of a protein molecule move and interact and how these various motions are directed in a concerted way by the protein structure and interatomic/intermolecular forces to allow proteins to perform their function. My research is focused on the development and application of various physical, chemical, and biochemical approaches, both experimental and theoretical, to obtain high-resolution structures of protein molecules and accurately analyze their dynamics. The objective is to combine the structural and dynamics information in order to determine the "four-dimensional" (three spatial coordinates + time) structure of protein molecules. Current research includes development of new methods and further improvement in the existing approaches to (A) structure determination in multi-domain proteins and protein complexes and (B) protein dynamics, using Nuclear Magnetic Resonance (NMR) and relaxation, molecular dynamics simulations, and physical and mathematical modeling. These methods have been applied to determine the inter-domain orientation and interactions in multi-domain proteins involved in intracellular signal transduction. Key words: protein structure, protein dynamics, nuclear magnetic resonance, NMR, spin relaxation, molecular dynamics simulations. |