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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6333
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pubmed:dateCreated |
1991-8-22
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pubmed:abstractText |
A new system has been developed for measuring the forces produced by a small number (less than 5-150) of myosin molecules interacting with a single actin filament in vitro. The technique can resolve forces of less than a piconewton and has a time resolution in the submillisecond range. It can thus detect fluctuations of force caused by individual molecular interactions. From analysis of these force fluctuations, the coupling between the enzymatic ATPase activity of actomyosin and the resulting mechanical impulses can be elucidated.
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pubmed:commentsCorrections | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
|
pubmed:issn |
0028-0836
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
25
|
pubmed:volume |
352
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
301-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1830130-Actins,
pubmed-meshheading:1830130-Actomyosin,
pubmed-meshheading:1830130-Adenosine Triphosphatases,
pubmed-meshheading:1830130-Humans,
pubmed-meshheading:1830130-Mathematics,
pubmed-meshheading:1830130-Methods,
pubmed-meshheading:1830130-Muscle Contraction,
pubmed-meshheading:1830130-Myosins
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pubmed:year |
1991
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pubmed:articleTitle |
Sub-piconewton force fluctuations of actomyosin in vitro.
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pubmed:affiliation |
Department of Biophysical Engineering, Osaka University, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|