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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
17
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pubmed:dateCreated |
2009-5-6
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pubmed:abstractText |
Structural integrity as well as mechanical stability of the parts of a molecular motor are crucial for its function. In this study, we used high-resolution force spectroscopy by atomic force microscopy to investigate the force-dependent opening kinetics of the neck coiled coil of Kinesin-1 from Drosophila melanogaster. We find that even though the overall thermodynamic stability of the neck is low, the average opening force of the coiled coil is >11 pN when stretched with pulling velocities >150 nm/s. These high unzipping forces ensure structural integrity during motor motion. The high mechanical stability is achieved through a very narrow N-terminal unfolding barrier if compared with a conventional leucine zipper. The experimentally mapped mechanical unzipping profile allows direct assignment of distinct mechanical stabilities to the different coiled-coil subunits. The coiled-coil sequence seems to be tuned in an optimal way to ensure both mechanical stability as well as motor regulation through charged residues.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19369199-10329654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19369199-10485889,
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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 |
Apr
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
28
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pubmed:volume |
106
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6992-7
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pubmed:dateRevised |
2010-9-27
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pubmed:meshHeading |
pubmed-meshheading:19369199-Amino Acid Sequence,
pubmed-meshheading:19369199-Animals,
pubmed-meshheading:19369199-Drosophila melanogaster,
pubmed-meshheading:19369199-Humans,
pubmed-meshheading:19369199-Kinesin,
pubmed-meshheading:19369199-Models, Molecular,
pubmed-meshheading:19369199-Molecular Sequence Data,
pubmed-meshheading:19369199-Protein Structure, Secondary,
pubmed-meshheading:19369199-Protein Structure, Tertiary,
pubmed-meshheading:19369199-Sequence Alignment
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pubmed:year |
2009
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pubmed:articleTitle |
Single molecule mechanics of the kinesin neck.
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pubmed:affiliation |
Physics Department E22, Technische Universität München, James Franck Strasse, 85748 Garching, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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