The myosin motor in muscle generates a smaller and slower working stroke at higher load View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-04

AUTHORS

Massimo Reconditi, Marco Linari, Leonardo Lucii, Alex Stewart, Yin-Biao Sun, Peter Boesecke, Theyencheri Narayanan, Robert F. Fischetti, Tom Irving, Gabriella Piazzesi, Malcolm Irving, Vincenzo Lombardi

ABSTRACT

Muscle contraction is driven by the motor protein myosin II, which binds transiently to an actin filament, generates a unitary filament displacement or ‘working stroke’, then detaches and repeats the cycle. The stroke size has been measured previously using isolated myosin II molecules at low load, with rather variable results1,2,3,4, but not at the higher loads that the motor works against during muscle contraction. Here we used a novel X-ray-interference technique5,6 to measure the working stroke of myosin II at constant load7 in an intact muscle cell, preserving the native structure and function of the motor. We show that the stroke is smaller and slower at higher load. The stroke size at low load is likely to be set by a structural limit8,9; at higher loads, the motor detaches from actin before reaching this limit. The load dependence of the myosin II stroke is the primary molecular determinant of the mechanical performance and efficiency of skeletal muscle. More... »

PAGES

578-581

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature02380

DOI

http://dx.doi.org/10.1038/nature02380

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1035802914

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15058307


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