Nulceotide-dependent single-to double-headed binding of kinesin

The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesing 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'-triphosphat...

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Bibliographic Details
Published inScience (American Association for the Advancement of Science) Vol. 291; no. 5504; pp. 667 - 669
Main Authors Kawaguchi, Kenji, Ishiwata, Shin-ichi
Format Journal Article
LanguageEnglish
Published Washington The American Association for the Advancement of Science 26.01.2001
Subjects
Crystals
Evidence
Kinetics
Membranes
Molecules
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Summary:The motility of kinesin motors is explained by a "hand-over-hand" model in which two heads of kinesing 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 comples by applying an external load with optical tweezers.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
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ISSN:0036-8075
1095-9203