Linked Life Data

8089077

Source:http://linkedlifedata.com/resource/pubmed/id/8089077

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1994-10-18
pubmed:abstractText
In order to determine the relative motions of an actin filament and a myosin molecule upon hydrolysis of one ATP, an in vitro motility assay, in which individual actin filaments slide over heavy meromyosin molecules bound to a substrate, was combined with an optical trapping technique. An actin filament, attached to a gelsolin-coated bead, was captured with an optical trap. The surface-bound heavy meromyosin molecules pulled the filament against the trapping force, which resulted in back and forth motions of the actin-bound bead. The number of heavy meromyosin molecules interacting with an actin filament (at most 1/micron filament) and the ATP concentration (< or = 0.5 microM) were chosen so as to facilitate detection of each "pull." Calculation of the centroid of the bead image revealed abrupt displacements of the actin filament. The frequency of such displacements was between 0.05 and 0.1 per 1 s per 1 micron actin filament, being consistent with calculated values based on the reported bimolecular binding constants of ATP and the actomyosin rigor complex. The distribution of the displacements peaked around 7 nm at a trapping force of 0.016 pN/nm, but it became broader, and some displacements were as large as 30 nm, when the trapping force was reduced to 0.0063 pN/nm, suggesting that the force generation due to the structural change of a myosin head may be insufficient to explain such displacements.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
644-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Stepwise motion of an actin filament over a small number of heavy meromyosin molecules is revealed in an in vitro motility assay.
pubmed:affiliation
Department of Physics, Faculty of Science and Technology, Keio University, Kanagawa.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't