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Mechanochemical couplings of kinesin motors.

作者信息

Xie Ping, Dou Shuo-Xing, Wang Peng-Ye

机构信息

Laboratory of Soft Matter Physics, Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.

出版信息

Biophys Chem. 2006 Aug 20;123(1):58-76. doi: 10.1016/j.bpc.2006.04.003. Epub 2006 Apr 26.

DOI:10.1016/j.bpc.2006.04.003
PMID:16707205
Abstract

Kinesins are molecular motors capable of moving processively along microtubule in a stepwise manner by hydrolyzing ATP. Numerous experimental results on various aspects of their dynamical behaviours are available in literature. Although a number of models of tightly coordinated mechanism have been proposed to explain some experimental results, up to now no good explanation has been given to all these experimental results by using a single model. We have recently proposed such a model of partially coordinated hand-over-hand moving mechanism. In this paper, we use this model to study in detail various aspects of the dynamical properties of single kinesin molecules. We show that kinesin dimers walk hand-over-hand along microtubules in a partially coordinated rather than a tightly coordinated manner. The degree of coordination depends on the ratio of the two heads' ATPase rates that are in turn determined by both internal elastic force and external load. We have tested this model using various available experimental results on different samples and obtained a good agreement between the theory and the experiments.

摘要

相似文献

1
Mechanochemical couplings of kinesin motors.
Biophys Chem. 2006 Aug 20;123(1):58-76. doi: 10.1016/j.bpc.2006.04.003. Epub 2006 Apr 26.
2
Model for kinetics of wild-type and mutant kinesins.野生型和突变型驱动蛋白的动力学模型。
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Nucleotide-dependent single- to double-headed binding of kinesin.驱动蛋白的核苷酸依赖性单头至双头结合
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Loading direction regulates the affinity of ADP for kinesin.负载方向调节二磷酸腺苷对驱动蛋白的亲和力。
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Kinesin's backsteps under mechanical load.驱动蛋白在机械负载下的后退步。
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