|
Title: The motion cycle of myosin II: Computational approaches
Abstract:
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 elucidated, small changes in the ATP binding site are communicated to a distant force-generating domain, resulting in a large conformational change. This conformational change is coupled to actin binding and release in a cycle that ultimately generates muscle contraction. Crystal structures of myosin II end-states in the contractile cycle are now available in high resolution. We propose a number of computational methods to generate meaningful intermediates connecting the two end-states. |
