Tilting of the light-chain region of myosin during step length changes and active force generation in skeletal muscle

Article Abstract:

Filament sliding and force generation in skeletal muscle is probably aided by myosin crossbridges, as shown by fluorescence polarization which documented the myosin head tilting. The myosin light-chain region goes through structural, mechanical and biochemical states during muscle contraction and the myosin crossbridges have polarization changes that switch direction based on whether the muscle is in rigor or contraction. This evidence supports the tilting crossbridge model.

Muscles

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A fine time for contractual alterations

Article Abstract:

The head of a myosin molecule can reorient itself, filling the space between the thick (myosin) and the thin (actin) filaments, which in turn brings on muscular contraction by changing the mass projected onto the fiber axis. M. Irving and colleagues confirmed the process of muscular tension by subjecting a single muscle fiber to X-ray diffraction analysis. The research showed that the anticipated muscular changes go along with the 'working stroke' of the force generators.

Actin

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Crossbridge tilting confirmed

Article Abstract:

The tilting movement of the myosin molecules' heads during the working stroke of a muscle may be involved in the creation of a crossbridge between the thin and thick filaments of the muscle, causing relative sliding. There may be more than one component in the working stroke but evidence from electron micrographs of asynchronous insect flight muscles supports the myosin crossbridges as a factor.

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