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Chinese Physics, 2005, Vol. 14(4): 734-743    DOI: 10.1088/1009-1963/14/4/017
ATOMIC AND MOLECULAR PHYSICS Prev   Next  

Mechanism for unidirectional movement of kinesin

Xie Ping (谢平), Dou Shuo-Xing (窦硕星), Wang Peng-Ye (王鹏业)
Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China
Abstract  Kinesin motors have been studied extensively both experimentally and theoretically. However, the microscopic mechanism of the processive movement of kinesin is still an open question. In this paper, we propose a hand-over-hand model for the processivity of kinesin, which is based on chemical, mechanical, and electrical couplings. In the model the ATPase rates of the two kinesin heads are regulated by forces, both from internal elasticity and external load, exerted on their necks. At a low external load, the ATPase rate of the trailing head is much higher than the leading head and the two heads are coordinated in their ATP hydrolysis and mechanical cycles. The motor walks processively with one ATP being hydrolyzed per step. At a higher forward external load, the ATPase rates of the two heads become comparable and thus the two heads are no longer well coordinated in their ATP hydrolysis and mechanical cycles. The model is consistent with the structural study of kinesin and the measured pathway of the kinesin ATPase. Using the model we have estimated the driving force to be $\sim$5.8pN, which is in agreement with the experimental results (5--7.5pN). The estimated time for moving one step ($\sim$10$\mu$s) is also consistent with the measured values of 0--50$\mu$s. The previous observation of substeps within the 8nm step is explained. The shapes of velocity versus load (both positive and negative) curves show close resemblance to previous experimental results.
Keywords:  kinesin      molecular motor      mechanism      dynamics  
Received:  21 May 2004      Revised:  11 August 2004      Accepted manuscript online: 
PACS:  87.15.B- (Structure of biomolecules)  
  87.15.H- (Dynamics of biomolecules)  
  87.16.Nn (Motor proteins (myosin, kinesin dynein))  
  87.15.R- (Reactions and kinetics)  
  87.15.La (Mechanical properties)  
  87.15.A- (Theory, modeling, and computer simulation)  
Fund: Project supported by the National Natural Science Foundation of China (Grant Nos 60025516, 10334100)

Cite this article: 

Xie Ping (谢平), Dou Shuo-Xing (窦硕星), Wang Peng-Ye (王鹏业) Mechanism for unidirectional movement of kinesin 2005 Chinese Physics 14 734

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