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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Basic Research in Ca...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Basic Research in Cardiology
Article . 1974 . Peer-reviewed
License: Springer TDM
Data sources: Crossref
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On the isometric equation of the sarcomere

Authors: Paul J. Lewi; Wolfgang Schaper; Ludo M. J. Gijpen;

On the isometric equation of the sarcomere

Abstract

A model of the sarcomere is described, which is based upon (a) the sliding filament theory ofHuxley, (b) the ultrastructure of the sarcomere, (c) the biochemical mechanisms responsible for mechanical coupling and uncoupling of myosin and actin, (d) the constancy of the volume of the sarcomere and (e) a statistical analysis of random forces acting on myosin cross-bridges, constrained by flexible and extensible heavy meromyosin subfragments. The results can be fitted to experimental Frank-Starling diagrams. Maximal velocity of contraction, derived from the theory, is independent of sarcomere length, while the rate of force generation is predicted to increase with increasing sarcomere length. The relationship of the new model with the older three-element models is discussed and a new definition of the series elastic element is proposed representing the series component as being distributed over the thin and elongated heavy meromyosin subfractions which connect the crossbridges to the myosin backbone.

Related Organizations
Keywords

Binding Sites, Myocardium, Physical Exertion, Myosin Subfragments, Heart, Myosins, Papillary Muscles, Models, Biological, Actins, Elasticity, Biomechanical Phenomena, Myofibrils, Humans, Calcium, Muscle Contraction

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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
0
Average
Average
Average
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