Contraction isometric force dependence

In terms of muscle function, muscle is very adaptable. Depending on the type of stimulation, muscle can either twitch or contract tetanically for a variable length of time. If the ends are held fixed, then it contracts isometrically and the force produced is maximal. If one or both ends of the muscle are not held fixed then the muscle is able to shorten. The muscle can shorten at a fixed load (isotonic contraction) where the velocity of shortening is also constant. Power output (force X velocity) is maximum where the velocity of shortening is about one third of the maximal rate. Finally, the muscle can shorten at maximum velocity (unloaded shortening). However, the molecular basis of the interaction of myosin with actin to produce force, or shortening, is the same in each case. 

Both RLC phosphorylation and active stiffness increase more rapidly than isometric force during the initiation of the contraction (Kamm and Stull, 1986). These observations suggest that phosphorylation of myosin RLC allows cross-bridge attachment to actin. The delay in force development may result from cooperative effects of phosphorylation on activation whereby force depends on formation of doubly phos-phorylated myosin (Persechini and Hartshorne, 1981 Sellers et al., 1983) however, other contributions, including a delay in the expression of force through series elastic element in the tissue, cannot be excluded (Aksoyetfl/., 1983). 

The modeling and control of movements in this chapter relates to external control of muscles via so-called functional electrical stimulation. Macroscopic viscoelastic models started from the observation that the process of electrical stimulation transforms the viscoelastic material from a compliant, fluent state into the stiff, viscous state. Levin and Wyman [35] proposed a three-element model— damped and undamped elastic element in series. Hill s work [36] demonstrated that the heat transfer depends upon the type of contraction (isometric, slow contracting, etc). The model includes the force generator, damping and elastic elements. Winters [37] generalized Hill s model in a simple enhancement of the original, which... 

The development of force under conditions of fixed length, as in an isometric contraction, involves the elastic deformation of a chain or chains within the protein-based machine. On relaxation, ideal elastic elements return the total energy of deformation to the protein-based machine for the performance of mechanical work. Thus, the approach toward high efficiency for the function of a protein-based linear motor, or even for the RIP domain movement in Complex III, depends on how nearly the extension of an elastomeric chain segment approaches ideal elasticity. 

Description of the mechanics of elastin requires the understanding of two interlinked but distinct physical processes the development of entropic elastic force and the occurrence of hydrophobic association. Elementary statistical-mechanical analysis of AFM single-chain force-extension data of elastin model molecules identifies damping of internal chain dynamics on extension as a fundamental source of entropic elastic force and eliminates the requirement of random chain networks. For elastin and its models, this simple analysis is substantiated experimentally by the observation of mechanical resonances in the dielectric relaxation and acoustic absorption spectra, and theoretically by the dependence of entropy on frequency of torsion-angle oscillations, and by classical molecular-mechanics and dynamics calculations of relaxed and extended states of the P-spiral description of the elastin repeat, (GVGVP) . The role of hydrophobic hydration in the mechanics of elastin becomes apparent under conditions of isometric contraction. 

Figure 3. Force-Velocity and Power-Balance relations in isotonic and isometric contractions (see also Supplementary Box 3). (a) Isotonic Force-Velocity and Power-Balance relations for two values of a. (b) Quantitative spectrum of the isotonic variables versus V lo. (c) Kinetic profiles of isometric contraction against a load of compliance C. (d) Spectrum of compliance-dependent variables in isometric twitch contractions, versus the final tension.

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