Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 125, Issue 10, Pages 2627-2635Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.1c00549
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Funding
- National Natural Science Foundation of China [11774284, 11904278]
- Shaanxi Science and Technology Project [2020JQ-612]
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This study develops a kinetic model that is quantitatively validated by experimental data, revealing the physical mechanism of kinesin stepping and its directionality regulated by a biased diffusion process. The results suggest that kinesin directionality is optimized through fulfilling a thermodynamic constraint.
Conventional kinesin is a high-performance motor that moves primarily toward the plus end of microtubules and occasionally toward the opposite direction. The physical mechanism of this directional stepping remains unclear. Here we develop a kinetic two-cycle model incorporating kinesin forward and backward stepping, in which the neck linker zippering and ATP catalysis process are conserved in backward steps. This model is quantitatively validated by a variety of experimental data, including load dependence of velocity, stepping ratio, and dwell time. The physical mechanism of kinesin stepping regulated by a biased diffusion process is identified by analyzing the load dependence and relevant thermodynamic properties of the model. Furthermore, the model suggests the kinesin directionality is optimized resulting from fulfilling a thermodynamic constraint. Our modeling provides a chemomechanical coupling mechanism that connects the flexibility of the neck linker zippering effect for direction rectification and the measured performance into a consistent frame.
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