驱动蛋白的内在抗负荷能力
The intrinsic load-resisting capacity of kinesin
摘要：
传统的驱动蛋白是一种同源二聚体马达蛋白，能够沿着细胞骨架丝单向行走。虽然以前的实验表明，不屈的单向性对相反的负载，所谓的失速力，最近的实验还观察到有限的超失速负载下的过程后退。这项理论研究旨在阐明驱动蛋白的步骤，可能被施加到二聚体的外部负载的全范围内的分子力学基础。我们发现，驱动蛋白的负荷抵抗能力在很大程度上是由二聚体固有的协同棘轮和棘爪机制。这种内部分子机械机制的负载敏感性是驱动蛋白对各种水平的外部负载的响应的基础。该机制的计算实现使我们能够合理化的主要趋势实验观察驱动蛋白的僵局和连续的后退步骤。该研究还预测了驱动蛋白的负荷影响运动的几个明显特征，这似乎是违反直觉的，但很容易通过未来的实验验证。
英文摘要：
Conventional kinesin is a homodimeric motor protein that is capable of walking unidirectionally along a cytoskeletal filament. While previous experiments indicated unyielding unidirectionality against an opposing load up to the so-called stall force, recent experiments also observed limited processive backwalking under superstall loads. This theoretical study seeks to elucidate the molecular mechanical basis for kinesin's steps over the full range of external loads that can possibly be applied to the dimer. We found that kinesin's load-resisting capacity is largely determined by a synergic ratchet-and-pawl mechanism inherent in the dimer. Load susceptibility of this inner molecular mechanical mechanism underlies kinesin's response to various levels of external loads. Computational implementation of the mechanism enabled us to rationalize major trends observed experimentally in kinesin's stalemate and consecutive back steps. The study also predicts several distinct features of kinesin's load-affected motility, which are seemingly counterintuitive but readily verifiable by future experiment.
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