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Mechanochemical model for myosin V

Craig, Erin M. and Linke, Heiner LU (2009) In Proceedings of the National Academy of Sciences 106(43). p.18261-18266
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Brownian dynamics, molecular motor, strain-dependent gating
in
Proceedings of the National Academy of Sciences
volume
106
issue
43
pages
18261 - 18266
publisher
National Acad Sciences
external identifiers
  • wos:000271222500041
  • scopus:70849119718
ISSN
1091-6490
DOI
10.1073/pnas.0908192106
language
English
LU publication?
yes
id
3025355f-5cc3-4900-9813-9be9f86be6ba (old id 1504720)
date added to LUP
2009-11-25 09:55:46
date last changed
2017-03-19 03:25:22
@article{3025355f-5cc3-4900-9813-9be9f86be6ba,
  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.},
  author       = {Craig, Erin M. and Linke, Heiner},
  issn         = {1091-6490},
  keyword      = {Brownian dynamics,molecular motor,strain-dependent gating},
  language     = {eng},
  number       = {43},
  pages        = {18261--18266},
  publisher    = {National Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {Mechanochemical model for myosin V},
  url          = {http://dx.doi.org/10.1073/pnas.0908192106},
  volume       = {106},
  year         = {2009},
}