I am currently a PhD candidate in Michael Levitt’s lab at Stanford University. My work focuses on computational methods designed to understand the dynamic motion pathway of myosin.

Myosin II is a motor protein that converts the chemical energy derived from ATP hydrolysis into mechanical energy. In a process that is not yet fully understood, small changes in the ATP binding site are communicated to a distant force-generating domain, resulting in a large conformational change. This conformational change ultimately generates muscle contraction.

Crystal structures of myosin II end-states in the contractile cycle are now available in high resolution. I would like to implement a number of methods to generate meaningful intermediates connecting the two end-states in order to visualize the entire motion pathway. I am also interested in developing a coarse-grained working model of myosin. I require that this model will have the same shape and vibrational properties as myosin, that it will require same amount of energy to move or bend the model as to move or bend the real molecule, and finally that the model will be able to predict or replicate the effects of point mutations.