Robert A. Welch Chair in Chemistry
University of Texas, Austin
Abstract: Myosin V, two-headed motor protein and a member of the myosin super family, ferries cellular cargo by walking hand-over-hand on actin filaments. Interplay between ATD-driven conformational changes in the motor head and stress due to load produces a variety of stepping dynamics: the motor can step forward or backward, or "stomp", where one of the heads detaches and rebinds to the same site. I will present theory that captures all these behaviors, quantitatively matching a wide array of single molecule experiments. The theory lays out the structural and chemical design principles underlying the motor's robust function, which provides a guide for how bioengineering might alter its dynamics . The theoretical results will be complemented with simulations describing the role the internal dynamics of the motor domain plays in motility .
 M. Hinczewski, R. Tehver, and D. Thirumalai, Proc. Natl. Acad. Sci. 110: E4059-E4068, (2013).
 R. Tehver and D. Thirumalai, Structure, 18: 471-481, (2010).