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PMID: 8139653 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Single myosin molecule mechanics: piconewton forces and nanometre steps.

Nature ·Vol. 368 ·No. 6467 ·1994-03-10 ·Pages 113-9

Finer JT, Simmons RM, Spudich JA

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.

MeSH Terms
Actins/physiology Adenosine Triphosphate/physiology Animals Biomechanical Phenomena Feedback In Vitro Techniques Myosin Subfragments Myosins/physiology Rabbits
Chemicals
Actins Myosin Subfragments Adenosine Triphosphate Myosins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Finer J T
Department of Biochemistry, Beckman Center, Stanford University School of Medicine, California 94305.
Simmons R M
Spudich J A
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1994-03-10
Pages
113-9
Language
English
Region
England
NLM ID
0410462
Subset
IM
Grants
Wellcome Trust · United Kingdom
Corrections
CommentIn
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