Peskin C S, Oster G
Courant Institute of Mathematical Sciences, New York, New York 10012, USA.
Biophys J. 1995 Apr;68(4 Suppl):202S-210S; discussion 210S-211S.
The two-headed motor protein kinesin hydrolyzes nucleotide to move unidirectionally along its microtubule track at speeds up to 1000 nm/s (Saxton et al., 1988) and develops forces in excess of 5 pN (Hunt et al., 1994; Svoboda et al., 1994a). Individual kinesin molecules have been studied recently in vitro, and their behavior has been characterized in terms of force-velocity curves and variance measurements (Svoboda and Block, 1994a; Svoboda et al., 1994b). We present a model for force generation in kinesin in which the ATP hydrolysis reactions are coordinated with the relative positions of the two heads. The model explains the experimental data and permits us to study the relative roles of Brownian motion and elastic deformation in the motor mechanism of kinesin.
双头马达蛋白驱动蛋白通过水解核苷酸沿着微管轨道单向移动，速度可达1000 nm/s（萨克斯顿等人，1988年），并产生超过5皮牛的力（亨特等人，1994年；斯沃博达等人，1994年a）。最近对单个驱动蛋白分子进行了体外研究，其行为已根据力-速度曲线和方差测量进行了表征（斯沃博达和布洛克，1994年a；斯沃博达等人，1994年b）。我们提出了一个驱动蛋白中力产生的模型，其中ATP水解反应与两个头部的相对位置相协调。该模型解释了实验数据，并使我们能够研究布朗运动和弹性变形在驱动蛋白运动机制中的相对作用。
