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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-3-1
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pubmed:abstractText |
Conventional kinesin has a double-headed structure consisting of two motor domains and moves processively along a microtubule using the two heads cooperatively. The movement of single and multiple truncated heads of Drosophila kinesin was measured using a laser trap and nanometer detecting apparatus. Single molecules of single-headed kinesin bound to the microtubules with a 3.5 nm biased displacement toward the plus end of the microtubule. The position of these single-headed kinesin molecules bound to a microtubule did not change until they had dissociated, indicating that single kinesin heads utilize nonprocessive movement processes. Two molecules of single-headed kinesin moved continuously along a microtubule with a lower velocity and force than that of single molecules of double-headed kinesin. The biased binding of the heads determines the directionality of movement, whereas two molecules of single-headed kinesin move continuously without dissociation from a microtubule.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10024239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10206648,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10441125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10545098,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10557288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10617199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10639132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10753125,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-10972296,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-11025663,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-11283618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-11373668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-11606295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-12351789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-12360289,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-12640444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-12891363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-14634664,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-14657506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-14684828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-15257294,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-2530455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-2911722,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-3130248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-3134048,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-7854458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-8205624,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-8246791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-8413650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-9207081,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/15626711-9521668
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3495
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2068-77
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15626711-Animals,
pubmed-meshheading:15626711-Binding Sites,
pubmed-meshheading:15626711-Computer Simulation,
pubmed-meshheading:15626711-Drosophila,
pubmed-meshheading:15626711-Kinesin,
pubmed-meshheading:15626711-Microtubules,
pubmed-meshheading:15626711-Models, Chemical,
pubmed-meshheading:15626711-Models, Molecular,
pubmed-meshheading:15626711-Molecular Motor Proteins,
pubmed-meshheading:15626711-Motion,
pubmed-meshheading:15626711-Protein Binding,
pubmed-meshheading:15626711-Stress, Mechanical,
pubmed-meshheading:15626711-Structure-Activity Relationship,
pubmed-meshheading:15626711-Swine
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pubmed:year |
2005
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pubmed:articleTitle |
Biased binding of single molecules and continuous movement of multiple molecules of truncated single-headed kinesin.
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pubmed:affiliation |
Department of Metallurgy, School of Engineering, Tohoku University, Sendai 980-8579, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't,
Evaluation Studies
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