Our research involves the elucidation of the structure, dynamics and function of proteins; including the role of intrinsically unfolded regions in regulating biological interactions. The major systems focus of our research is cardiovascular disease. In particular, we are interested in the function of the proteins that make up the thin filament of skeletal and cardiac muscle and regulate contraction; focusing on the calcium sensitive interactions between actin, tropomyosin, and troponin. We are presently studying the effects of drug binding, phosphorylation, acidosis and FHC mutations in the cardiac system. Our major tool is nuclear magnetic resonance spectroscopy, especially the use of multi-nuclear and multi-dimensional NMR techniques combined with the computational techniques of energy minimization and molecular dynamics to determine the structure of proteins in solution. We are also studying prion proteins in order to understand the mechanism of the conversion from the cellular to the Scrapie form; using NMR based metabolomic studies to diagnose human disease; and developing NMR methods for the study of the structure of membrane proteins.