We employ optical spectroscopic techniques to study dynamics and structure of contractile proteins. Techniques include:

1. time-resolved fluorescence polarization microscopy measuring rotational dynamics of fluorescent labeled proteins on the microsecond or longer time scale;
2. steady-state and time-resolved fluorescence spectroscopy looking at protein structure and dynamics, and;
3. circular dichroism (CD) quantifying polypeptide and protein tertiary structure in the steady-state.

The CD studies have a nuclear magnetic resonance (NMR) and a computational chemistry component dedicated to interpreting CD spectra in terms of atomic structure.

The biologically interesting system we study is the actin/myosin (actomyosin) complex at the heart of the contractile apparatus. It is the unitary force producing element in a majority of things that move in living creatures. Myosin is the ATPase responsible for converting the chemical energy in ATP into mechanical work, i.e., it is the energy transducer. Actin is the myosin substrate that has work done on it. We use the intact skeletal muscle fiber system to look at myosin orientation dynamics during contraction and muscle shortening. Structural studies are performed on the isolated proteins in solution. The chief aim of the research is to structurally characterize myosin during contraction to elucidate the structural basis of its energy transduction mechanism.

Medical application of the research focuses on understanding how mutations in beta-cardiac myosin implicated in familial hypertrophic cardiomyopathy affects myosin function.