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Abstract: Conventional kinesin is a homodimeric motor protein that is capable ofwalking unidirectionally along a cytoskeletal filament. While previousexperiments indicated unyielding unidirectionality against an opposing load upto the so-called stall force, recent experiments also observed limitedprocessive backwalking under superstall loads. This theoretical study seeks toelucidate the molecular mechanical basis for kinesin-s steps over the fullrange of external loads that can possibly be applied to the dimer. We foundthat kinesin-s load-resisting capacity is largely determined by a synergicratchet-and-pawl mechanism inherent in the dimer. Load susceptibility of thisinner molecular mechanical mechanism underlies kinesin-s response to variouslevels of external loads. Computational implementation of the mechanism enabledus to rationalize major trends observed experimentally in kinesin-s stalemateand consecutive back steps. The study also predicts several distinct featuresof kinesin-s load-affected motility, which are seemingly counterintuitive butreadily verifiable by future experiment.

Autor: Wenwei Zheng, Dagong Fan, Min Feng, ZhisongWang


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