The efficiency of muscle contraction

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dc.contributor.author Smith, Nicolas en
dc.contributor.author Barclay, Christopher en
dc.contributor.author Loiselle, Denis en
dc.date.accessioned 2011-09-06T22:00:27Z en
dc.date.issued 2005 en
dc.identifier.citation Prog Biophys Mol Biol 88(1):1-58 May 2005 en
dc.identifier.issn 0079-6107 en
dc.identifier.uri http://hdl.handle.net/2292/7827 en
dc.description.abstract When a muscle contracts and shortens against a load, it performs work. The performance of work is fuelled by the expenditure of metabolic energy, more properly quantified as enthalpy (i.e., heat plus work). The ratio of work performed to enthalpy produced provides one measure of efficiency. However, if the primary interest is in the efficiency of the actomyosin cross-bridges, then the metabolic overheads associated with basal metabolism and excitation–contraction coupling, together with those of subsequent metabolic recovery process, must be subtracted from the total heat and work observed. By comparing the cross-bridge work component of the remainder to the Gibbs free energy of hydrolysis of ATP, a measure of thermodynamic efficiency is achieved. We describe and quantify this partitioning process, providing estimates of the efficiencies of selected steps, while discussing the errors that can arise in the process of quantification. The dependence of efficiency on animal species, fibre-type, temperature, and contractile velocity is considered. The effect of contractile velocity on energetics is further examined using a two-state, Huxley-style, mathematical model of cross-bridge cycling that incorporates filament compliance. Simulations suggest only a modest effect of filament compliance on peak efficiency, but progressively larger gains (vis-a-vis the rigid filament case) as contractile velocity approaches " Vmax: This effect is attributed primarily to a reduction in the component of energy loss arising from detachment of cross-bridge heads at non-zero strain. en
dc.language EN en
dc.relation.ispartofseries Progress in Biophysics & Molecular Biology en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/0079-6107/ en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.subject energy en
dc.subject enthalpy en
dc.subject efficiency en
dc.subject cross-bridges en
dc.subject fibre-type en
dc.subject species-differences en
dc.subject DOGFISH SCYLIORHINUS-CANICULA en
dc.subject CROSS-BRIDGE MODEL en
dc.subject DISTRIBUTION-MOMENT MODEL en
dc.subject FROG SKELETAL-MUSCLE en
dc.subject SLOW-TWITCH MUSCLES en
dc.subject X-RAY-DIFFRACTION en
dc.subject CREATINE-KINASE EQUILIBRIUM en
dc.subject NUCLEAR MAGNETIC-RESONANCE en
dc.subject MYOSIN ISOFORM COMPOSITION en
dc.subject ATP HYDROLYSIS EQUILIBRIA en
dc.title The efficiency of muscle contraction en
dc.type Journal Article en
dc.identifier.doi 10.1016/j.pbiomolbio.2003.11.014 en
pubs.issue 1 en
pubs.begin-page 1 en
pubs.volume 88 en
dc.rights.holder Copyright: 2003 Elsevier Ltd. en
dc.identifier.pmid 15561300 en
pubs.end-page 58 en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 7882 en
pubs.org-id Bioengineering Institute en
pubs.org-id ABI Associates en
pubs.record-created-at-source-date 2010-09-01 en
pubs.dimensions-id 15561300 en


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