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Biophys. J. BioFAST: First Published March 25, 2005. doi:10.1529/biophysj.104.046763
© 2005 by the Biophysical Society.

A more recent version of this article appeared on June 1, 2005.
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BIOPHYSICAL THEORY AND MODELING

Elastic lever arm model for myosin V

Andrej Vilfan 1*

1 J. Stefan Institute

* To whom correspondence should be addressed. E-mail: andrej.vilfan{at}ijs.si.

Submitted on June 1, 2004
Revised on September 9, 2004
Accepted on 10 March 2005


  Abstract
We present a mechanochemical model for myosin V, a two-headed processive motor protein. We derive the properties of a dimer from those of an individual head, which we model both with a 4-state cycle (detached, attached with ADP. Pi, attached with ADP and attached without nucleotide) and alternatively with a 5-state cycle (where the power stroke is not tightly coupled to the phosphate release). In each state the lever arm leaves the head at a different, but fixed, angle. The lever arm itself is described as an elastic rod. The chemical cycles of both heads are coordinated exclusively by the mechanical connection between the two lever arms. Both models reproduce the observed hand-over-hand motion and fit the measured force-velocity relations. The main difference between the two models concerns the load dependence of the run length, which is much weaker in the 5-state model. We show how systematic processivity measurement under varying conditions could be used to distinguish between both models and to determine the kinetic parameters.

Key Words: Actin, Chemical kinetics, Motor proteins, Myosin V, Semiflexible polymers, Theory




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Copyright © 2005 by the Biophysical Society.