Albany 2015:Book of Abstracts

Albany 2015
Conversation 19
June 9-13 2015
©Adenine Press (2012)

Design principles governing the motility of myosin motors

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 (Hinczewski et al., 2013) The theoretical results will be complemented with simulations describing the role the internal dynamics of the motor domain plays in motility (Tehver and Thirumalai, 2010).

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

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

Dave Thirumalai

Institute for Physical Science and Technology
University of Maryland
, College Park, MD 20742

Ph: 301-405-4803
FAX 301-314-9404