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- Kenji Kawaguchi
- Department of Physics, School of Science and Engineering;
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- Shin'ichi Ishiwata
- Department of Physics, School of Science and Engineering;
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説明
<jats:p>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.</jats:p>
収録刊行物
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- Science
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Science 291 (5504), 667-669, 2001-01-26
American Association for the Advancement of Science (AAAS)
