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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Dynamic conformational changes due to the ATP hydrolysis in the motor domain of myosin: 10-ns molecular dynamics simulations.
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Dynamic conformational changes due to the ATP hydrolysis in the motor domain of myosin: 10-ns molecular dynamics simulations.

机译：由于肌球蛋白运动域中ATP水解而引起的动态构象变化：10 ns分子动力学模拟。

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摘要

Muscle contraction is caused by directed movement of myosin heads along actin filaments. This movement is triggered by ATP hydrolysis, which occurs within the motor domain of myosin. The mechanism for this intramolecular process remains unknown owing to a lack of ways to observe the detailed motions of each atom in the myosin molecule. We carried out 10-ns all-atom molecular dynamics simulations to investigate the types of dynamic conformational changes produced in the motor domain by the energy released from ATP hydrolysis. The results revealed that the thermal fluctuations modulated by perturbation of ATP hydrolysis are biased in one direction that is relevant to directed movement of the myosin head along the actin filament.
机译：肌肉收缩是由肌球蛋白头沿肌动蛋白丝的定向运动引起的。该运动由ATP水解触发，ATP水解发生在肌球蛋白的运动域内。由于缺乏观察肌球蛋白分子中每个原子的详细运动的方法，这种分子内过程的机制仍然未知。我们进行了10 ns的全原子分子动力学模拟，以研究ATP水解释放的能量在运动域中产生的动态构象变化类型。结果表明，由ATP水解扰动调节的热波动偏向与肌球蛋白头沿肌动蛋白丝定向运动有关的一个方向。

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