Kinesin is a protein belonging to a class of motor proteins found in eukaryotic cells. Kinesins move along microtubule filaments, and are powered by the hydrolysis of ATP. A lot of salt bridges present between motor and microtubule. The salt bridge energy calculation was calculated in the way of the electrostatic interaction energy calculation. According to the results of the salt bridge, we obtain the quantitative difference in the binding energies for the salt bridge between the ATP state and ADP state is -68.01kJ/mol. This result indicates that the binding strength of kinesin at ATP state is really much bigger than that at the ADP state. This result is qualitatively in accordance with experiment. Through the research and analysis of the system of microtubule-based molecular motors (kinesin) at the microscopic level, we have got a deeper understanding of the mechanism of kinesin's walking along microtubule.%驱动蛋白是一种ATP酶,属于一种在真核细胞中发现的马达蛋白类,驱动蛋白通过ATP的水解供能,能够沿着微管正向运动.驱动蛋白与微管之间存在着盐键相互作用力,在本文中采取静电相互作用方式来对驱动蛋白与微管之间的盐键键能量进行定量计算,根据计算的数据结果做了一个在ATP强结合态和ADP弱结合态两个态下的氢键统计分析,得到强结合态与弱结合态的能量相差-68.01 kJ/mol,表明驱动蛋白处于ATP结合态时与微管的相互作用确实明显强于ADP结合态,这个结果与有关的实验事实定性地吻合.通过对微管上的驱动蛋白微观水平上的研究和分析,加深了对于驱动蛋白沿微管运动的机理的理解.
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