Journal
ANNALS OF BIOMEDICAL ENGINEERING
Volume 36, Issue 10, Pages 1624-1640Publisher
SPRINGER
DOI: 10.1007/s10439-008-9536-6
Keywords
muscle; contraction; lattice; filaments; compliance
Categories
Funding
- National Institutes of Health [R01 AR048776]
- Wellcome Trust [07002]
- Medical Research Council (UK)
- MRC [G0300412] Funding Source: UKRI
- Medical Research Council [G0300412] Funding Source: researchfish
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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.
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