Towards a Unified Theory of Muscle Contraction. I: Foundations

Smith, D.A. and Geeves, Michael A. and Sleep, J. and Mijailovich, Srboljub M. (2008) Towards a Unified Theory of Muscle Contraction. I: Foundations. Annals of Biomedical Engineering, 36 (10). pp. 1624-1640. ISSN 0090-6964 . (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Official URL
http://dx.doi.org/10.1007/s10439-008-9536-6

Abstract

Molecular models of contractility in striated muscle require an integrated description of the action of myosin motors, firstly in the filament lattice of the half-sarcomere. Existing models do not adequately reflect the biochemistry of the myosin motor and its sarcomeric environment. The biochemical actin-myosin-ATP cycle is reviewed, and we propose a model cycle with two 4- to 5-nm working strokes, where phosphate is released slowly after the first stroke. A smaller third stroke is associated with ATP-induced detachment from actin. A comprehensive model is defined by applying such a cycle to all myosin-S1 heads in the half-sarcomere, subject to generic constraints as follows: (a) all strain-dependent kinetics required for actin-myosin interactions are derived from reaction-energy landscapes and applied to dimeric myosin, (b) actin-myosin interactions in the half-sarcomere are controlled by matching rules derived from the structure of the filaments, so that each dimer may be associated with a target zone of three actin sites, and (c) the myosin and actin filaments are treated as elastically extensible. Numerical predictions for such a model are presented in the following paper.

Item Type: Article
Uncontrolled keywords: muscle; contraction; lattice; filaments; compliance
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Michael Geeves
Date Deposited: 15 May 2009 12:17
Last Modified: 15 Jul 2014 10:52
Resource URI: https://kar.kent.ac.uk/id/eprint/13224 (The current URI for this page, for reference purposes)
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