Single myosin molecule mechanics: piconewton forces and nanometre steps View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-03

AUTHORS

Jeffrey T. Finer, Robert M. Simmons, James A. Spudich

ABSTRACT

A new in vitro assay using a feedback enhanced laser trap system allows direct measurement of force and displacement that results from the interaction of a single myosin molecule with a single suspended actin filament. Discrete stepwise movements averaging 11 nm were seen under conditions of low load, and single force transients averaging 3–4 pN were measured under isometric conditions. The magnitudes of the single forces and displacements are consistent with predictions of the conventional swinging-crossbridge model of muscle contraction. More... »

PAGES

113-119

Journal

TITLE

Nature

ISSUE

6467

VOLUME

368

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/368113a0

DOI

http://dx.doi.org/10.1038/368113a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1049237121

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8139653


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197 grid-institutes:grid.168010.e schema:alternateName Departments of Biochemistry and Developmental Biology, Beckman Center, Stanford University School of Medicine, 94305, Stanford, California, USA
198 schema:name Departments of Biochemistry and Developmental Biology, Beckman Center, Stanford University School of Medicine, 94305, Stanford, California, USA
199 rdf:type schema:Organization
 




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