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Molecules 2019, 24(2), 287; https://doi.org/10.3390/molecules24020287

Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors

1,2
,
1,2
,
1,2,3
and
1,2,*
1
Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China
2
School of Physical Sciences, University of Chinese Academy of Sciences, Beijing 100049, China
3
Songshan Lake Materials Laboratory, Dongguan, Guangdong 523808, China
*
Author to whom correspondence should be addressed.
Received: 3 December 2018 / Revised: 10 January 2019 / Accepted: 11 January 2019 / Published: 14 January 2019
PDF [1646 KB, uploaded 14 January 2019]   |  

Abstract

Kinesin-1, kinesin-2 and kinesin-5 are three families of a superfamily of motor proteins; which can walk processively on microtubule filaments by hydrolyzing ATP. It was experimentally shown that while the three kinesin dimers show similar feature on the force dependence of velocity, they show rather different features on the force dependence of run length. However, why the three families of kinesins show these rather different features is unclear. Here, we computationally studied the movement dynamics of the three dimers based on our proposed model. The simulated results reproduce well the available experimental data on the force dependence of velocity and run length. Moreover, the simulated results on the velocity and run length for the three dimers with altered neck linker lengths are also in quantitative agreement with the available experimental data. The studies indicate that the three families of kinesins show much similar movement mechanism and the rather different features on the force dependence of run length arise mainly from the difference in rate constants of the ATPase activity and neck linker docking. Additionally, the asymmetric (limping) movement dynamics of the three families of homodimers with and without altered neck linker lengths are studied, providing predicted results.
Keywords: kinesin; processivity; velocity; chemomechanical coupling; motor protein kinesin; processivity; velocity; chemomechanical coupling; motor protein
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Guo, S.-K.; Wang, W.-C.; Wang, P.-Y.; Xie, P. Force Dependence of Velocity and Run Length of Kinesin-1, Kinesin-2 and Kinesin-5 Family Molecular Motors. Molecules 2019, 24, 287.

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