Document Detail


Mechanism of force generation by myosin heads in skeletal muscle.
MedLine Citation:
PMID:  11832949     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Muscles generate force and shortening in a cyclical interaction between the myosin head domains projecting from the myosin filaments and the adjacent actin filaments. Although many features of the dynamic performance of muscle are determined by the rates of attachment and detachment of myosin and actin, the primary event in force generation is thought to be a conformational change or 'working stroke' in the actin-bound myosin head. According to this hypothesis, the working stroke is much faster than attachment or detachment, but can be observed directly in the rapid force transients that follow step displacement of the filaments. Although many studies of the mechanism of muscle contraction have been based on this hypothesis, the alternative view-that the fast force transients are caused by fast components of attachment and detachment--has not been excluded definitively. Here we show that measurements of the axial motions of the myosin heads at ångström resolution by a new X-ray interference technique rule out the rapid attachment/detachment hypothesis, and provide compelling support for the working stroke model of force generation.
Authors:
Gabriella Piazzesi; Massimo Reconditi; Marco Linari; Leonardo Lucii; Yin-Biao Sun; Theyencheri Narayanan; Peter Boesecke; Vincenzo Lombardi; Malcolm Irving
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Nature     Volume:  415     ISSN:  0028-0836     ISO Abbreviation:  Nature     Publication Date:  2002 Feb 
Date Detail:
Created Date:  2002-02-08     Completed Date:  2002-03-13     Revised Date:  2012-02-22    
Medline Journal Info:
Nlm Unique ID:  0410462     Medline TA:  Nature     Country:  England    
Other Details:
Languages:  eng     Pagination:  659-62     Citation Subset:  IM    
Affiliation:
Università di Firenze, Viale G.B. Morgagni 63, I-50134 Firenze, Italy.
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MeSH Terms
Descriptor/Qualifier:
Animals
Biomechanics
Models, Biological
Molecular Motor Proteins / physiology
Muscle, Skeletal / physiology*
Myosins / physiology*
Rana temporaria
X-Ray Diffraction
Grant Support
ID/Acronym/Agency:
625//Telethon
Chemical
Reg. No./Substance:
0/Molecular Motor Proteins; EC 3.6.4.1/Myosins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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