Physics Colloquium

Prof. Dave Thirumalai, Department of Chemistry, UT Austin

"Design principles governing the motility of myosin motors in cells"

4:00pm, The John A. Wheeler Lecture Hall (RLM 4.102). Coffee and cookies will be served at 3:45pm in RLM 4.102

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 [1]. The theoretical results will be complemented with simulations describing the role the internal dynamics of the motor domain plays in motility [2].

References:
[1] M. Hinczewski, R. Tehver, and D. Thirumalai, Proc. Natl. Acad. Sci. 110:E4059-E4068, (2013).

[2] R. Tehver and D. Thirumalai, Structure, 18:471-481, (2010).