Mechanochemical model for myosin V
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1504720
- author
- Craig, Erin M. and Linke, Heiner LU
- organization
- publishing date
- 2009
- 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 Academy of Sciences
- external identifiers
-
- wos:000271222500041
- scopus:70849119718
- pmid:19822760
- 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
- 2016-04-01 11:44:29
- date last changed
- 2022-01-26 17:34:21
@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}}, keywords = {{Brownian dynamics; molecular motor; strain-dependent gating}}, language = {{eng}}, number = {{43}}, pages = {{18261--18266}}, publisher = {{National Academy of Sciences}}, series = {{Proceedings of the National Academy of Sciences}}, title = {{Mechanochemical model for myosin V}}, url = {{http://dx.doi.org/10.1073/pnas.0908192106}}, doi = {{10.1073/pnas.0908192106}}, volume = {{106}}, year = {{2009}}, }