驱动蛋白产生力的机制。
The mechanics of force generation by kinesin.
作者信息
Howard J
机构信息
Department of Physiology and Biophysics, University of Washington, Seattle 98195, USA.
出版信息
Biophys J. 1995 Apr;68(4 Suppl):245S-253S; 253S-255S.
Abstract
Several laboratories have developed highly sensitive mechanical techniques for studying the movement of purified motor proteins along their associated filaments. The aim of these experiments is to test models for force generation, such as the powerstroke model and "ratchet" or diffusional models, by 1) directly visualizing the path on the filament along which the motor moves, 2) measuring the force exerted by the motor against the filament, and 3) characterizing the passive mechanical properties (elasticity) of the motor. This paper focuses on recently published work on the microtubule-based motor kinesin taking this mechanical approach. Related work on myosin is mentioned for comparison.
摘要
几个实验室已经开发出高度灵敏的机械技术，用于研究纯化的运动蛋白沿着其相关细丝的运动。这些实验的目的是通过以下方式来测试力产生的模型，如动力冲程模型和“棘轮”或扩散模型：1）直接观察运动蛋白在细丝上移动的路径；2）测量运动蛋白对细丝施加的力；3）表征运动蛋白的被动机械特性（弹性）。本文重点关注最近发表的关于基于微管的驱动蛋白的采用这种机械方法的研究工作。为作比较，还提及了有关肌球蛋白的相关研究工作。
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The mechanics of force generation by kinesin.驱动蛋白产生力的机制。
Biophys J. 1995 Apr;68(4 Suppl):245S-253S; 253S-255S.
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本文引用的文献
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Muscle structure and theories of contraction.肌肉结构与收缩理论。
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Force of single kinesin molecules measured with optical tweezers.用光镊测量单个驱动蛋白分子的力。
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Recombinant kinesin motor domain binds to beta-tubulin and decorates microtubules with a B surface lattice.重组驱动蛋白运动结构域与β-微管蛋白结合，并以B表面晶格装饰微管。
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Nature. 1993 Jan 21;361(6409):269-71. doi: 10.1038/361269a0.
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Direct observation of kinesin stepping by optical trapping interferometry.通过光镊干涉测量法直接观察驱动蛋白的步移。
Nature. 1993 Oct 21;365(6448):721-7. doi: 10.1038/365721a0.
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Force-velocity relationships in kinesin-driven motility.驱动蛋白驱动的运动中的力-速度关系。
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10
Structure of the actin-myosin complex and its implications for muscle contraction.肌动蛋白-肌球蛋白复合物的结构及其对肌肉收缩的影响。
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