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• W2065168710 abstract "The motility of kinesin motors is explained by a “hand-over-hand” model in which two heads of kinesin alternately repeat single-headed and double-headed binding with a microtubule. To investigate the binding mode of kinesin at the key nucleotide states during adenosine 5′-triphosphate (ATP) hydrolysis, we measured the mechanical properties of a single kinesin-microtubule complex by applying an external load with optical tweezers. Both the unbinding force and the elastic modulus in solutions containing AMP-PNP (an ATP analog) were twice the value of those in nucleotide-free solution or in the presence of both AMP-PNP and adenosine 5′-diphosphate. Thus, kinesin binds through two heads in the former and one head in the latter two states, which supports a major prediction of the hand-over-hand model." @default.
• W2065168710 created "2016-06-24" @default.
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• W2065168710 date "2001-01-26" @default.
• W2065168710 modified "2023-10-18" @default.
• W2065168710 title "Nucleotide-Dependent Single- to Double-Headed Binding of Kinesin" @default.
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• W2065168710 doi "https://doi.org/10.1126/science.291.5504.667" @default.
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