Constitutive equations of skeletal muscle based on cross-bridge mechanism

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The cross-bridge cycle and skeletal muscle fatigue.

The functional correlates of fatigue observed in both animals and humans during exercise include a decline in peak force (P0), maximal velocity, and peak power. Establishing the extent to which these deleterious functional changes result from direct effects on the myofilaments is facilitated through understanding the molecular mechanisms of the cross-bridge cycle. With actin-myosin binding, the...

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Force and motion generated by skeletal muscle ultimately depends on the cyclical interaction of actin with myosin. This mechanical process is regulated by intracellular Ca(2+) through the thin filament-associated regulatory proteins i.e.; troponins and tropomyosin. Muscular dystrophies are a group of heterogeneous genetic affections characterized by progressive degeneration and weakness of the ...

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The Cross-Bridge of Skeletal Muscle Is Not Synchronized Either by Length or Force Step

Force and length steps, applied to a muscle fiber in the isometric state, are believed to synchronize attached cross-bridges. This alleged synchronization facilitates the interpretation of the experiments. A rapid force step elicits an elastic response of the attached cross-bridges, followed by an isotonic phase. The decay of this second isotonic phase is of the first order. This excludes that ...

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Evidence for cross-bridge order in contraction of glycerinated skeletal muscle.

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Muscle cross-bridge chemistry and force.

The recent article by Baker et al. (1999) presents a thermo-dynamic formalism that challenges the commonly held assumption that force production by muscle is localized to individual actin-bound myosin molecules. By assuming that the chemical reaction for the force-producing step is close enough to equilibrium to set ⌬G ϭ 0, the sum of the chemical and mechanical potentials of the products can b...

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ژورنال

عنوان ژورنال: Biophysical Journal

سال: 1985

ISSN: 0006-3495

DOI: 10.1016/s0006-3495(85)83895-9