ArticleRSC advances2019
A model for the chemomechanical coupling of myosin-V molecular motors.
Article in RSC advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- On the Control of Directionality of Myosin.Journal of the American Chemical Society · 2024Article
- Dynamics of ATP-dependent and ATP-independent steppings of myosin-V on actin: catch-bond characteristics.Journal of the Royal Society, Interface · 2020Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
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Abstract
Herein, a model for the chemomechanical coupling of dimeric myosin-V motors is presented. Based on this model and the proposal that the rate constants of the ATPase activity of the two heads are independent of an external force in a range smaller than the stall force, we analytically studied the dynamics of the motor, such as the stepping ratio, dwell time between two mechanical steps, and velocity, under varying force and ATP concentrations. The theoretical results well reproduce the diverse available single-molecule experimental data. In particular, the experimental data showing that at a low ATP concentration, the dwell time and velocity have less force dependency than at a high ATP concentration is explained quantitatively. Moreover, the dependency of the chemomechanical coupling ratio on the force and ATP concentration was studied.
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