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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
|
pubmed:dateCreated |
1998-7-27
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pubmed:abstractText |
A single molecule of F1-ATPase, a portion of ATP synthase, is by itself a rotary motor in which a central gamma subunit rotates against a surrounding cylinder made of alpha3beta3 subunits. Driven by three catalytic betas, each fueled with ATP, gamma makes discrete 120 degree steps, occasionally stepping backward. The work done in each step is constant over a broad range of imposed load and is close to the free energy of hydrolysis of one ATP molecule.
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pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0092-8674
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
26
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pubmed:volume |
93
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
1117-24
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:9657145-Actin Cytoskeleton,
pubmed-meshheading:9657145-Actins,
pubmed-meshheading:9657145-Adenosine Triphosphate,
pubmed-meshheading:9657145-Animals,
pubmed-meshheading:9657145-Bacillus,
pubmed-meshheading:9657145-Catalysis,
pubmed-meshheading:9657145-Microscopy, Fluorescence,
pubmed-meshheading:9657145-Microscopy, Video,
pubmed-meshheading:9657145-Proton-Translocating ATPases,
pubmed-meshheading:9657145-Rabbits,
pubmed-meshheading:9657145-Rotation
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pubmed:year |
1998
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pubmed:articleTitle |
F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps.
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pubmed:affiliation |
Department of Physics, Faculty of Science and Technology, Keio University, Yokohama, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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