Mechanochemical model for myosin V.

Abstract:

:A rigorous numerical test of a hypothetical mechanism of a molecular motor should model explicitly the diffusive motion of the motor's degrees of freedom as well as the transition rates between the motor's chemical states. We present such a Brownian dynamics, mechanochemcial model of the coarse-grain structure of the dimeric, linear motor myosin V. Compared with run-length data, our model provides strong support for a proposed strain-controlled gating mechanism that enhances processivity. We demonstrate that the diffusion rate of a detached motor head during motor stepping is self-consistent with known kinetic rate constants and can explain the motor's key performance features, such as speed and stall force. We present illustrative and realistic animations of motor stepping in the presence of thermal noise. The quantitative success and illustrative power of this type of model suggest that it will be useful in testing our understanding of a range of biological and synthetic motors.

authors

Craig EM,Linke H

doi

10.1073/pnas.0908192106

subject

Has Abstract

pub_date

2009-10-27 00:00:00

pages

18261-6

issue

43

eissn

0027-8424

issn

1091-6490

pii

0908192106

journal_volume

106

pub_type

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