期刊
SCIENCE
卷 291, 期 5504, 页码 667-669出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.291.5504.667
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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 tan 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.
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