The research goal of my laboratory is to understand the molecular interactions and structural dynamics of proteins involved in regulating contraction and relaxation of cardiac and skeletal muscle. We aim to determine the culprits of contractile dysfunction and remodeling in heart failure and muscle disorders, and then apply these insights to design novel therapies. We use biophysical approaches, such as time-resolved FRET (fluorescence resonance energy transfer) with site-directed probes on muscle proteins such actin, myosin, and myosin-binding protein C (MyBP-C), to assess mechanism of action. Currently, we are investigating the mechanism of action for effects of phosphorylation, disease-causing mutations, and small-molecule compounds on MyBP-C and its interactions with actin and myosin.
