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Origin of tradeoff between movement velocity and attachment duration of kinesin motor on a microtubule |
Yuying Liu(刘玉颖)1,† and Zhiqiang Zhang(张志强)2 |
1 Department of Physics, College of Science, China Agricultural University, Beijing 100083, China; 2 Basic Ministry, Space Engineering University, Beijing 101416, China |
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Abstract Kinesin-1 motor protein is a homodimer containing two identical motor domains connected by a common long coiled-coil stalk via two flexible neck linkers. The motor can step on a microtubule with a velocity of about 1 μm·s-1 and an attachment duration of about 1 s under physiological conditions. The available experimental data indicate a tradeoff between velocity and attachment duration under various experimental conditions, such as variation of the solution temperature, variation of the strain between the two motor domains, and so on. However, the underlying mechanism of the tradeoff is unknown. Here, the mechanism is explained by a theoretical study of the dynamics of the motor under various experimental conditions, reproducing quantitatively the available experimental data and providing additional predictions. How the various experimental conditions lead to different decreasing rates of attachment duration versus velocity is also explained.
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Received: 30 September 2023
Revised: 16 November 2023
Accepted manuscript online: 01 December 2023
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PACS:
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87.10.Tf
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(Molecular dynamics simulation)
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87.15.A-
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(Theory, modeling, and computer simulation)
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87.15.hg
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(Dynamics of intermolecular interactions)
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Corresponding Authors:
Yuying Liu
E-mail: liuyuying@cau.edu.cn
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Cite this article:
Yuying Liu(刘玉颖) and Zhiqiang Zhang(张志强) Origin of tradeoff between movement velocity and attachment duration of kinesin motor on a microtubule 2024 Chin. Phys. B 33 028708
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