myosin filaments

Note that the actin and myosin filaments themselves do not change length, but instead slide past each other.

The attached states are known as "cross bridges" between the actin and myosin filaments.

The interaction of sliding actin and myosin filaments is similar in smooth muscle.

The A band, on the other hand, contains mostly myosin filaments whose larger diameter restricts the passage of light.

ATP causes the binding between actin and myosin filaments to break.

All muscle cells are composed of a number of actin and myosin filaments in series.

Telokin may play a role in the stabilization of unphosphorylated smooth-muscle myosin filaments.

Myosin filaments have club-shaped heads that project toward the actin filaments.

Myosin filaments, the thick filaments, are bipolar and extend throughout the A-band.

This is due to reduced ability to cross-link actin and myosin filaments in over-stretched heart muscle.

As a result of the high calcium concentration, actin and myosin filaments will bind stronger, unable to relax properly to make a new contraction possible.

During muscle contraction, the heads of the myosin filaments attach to oppositely oriented thin filaments, actin, and pull them past one another.

The parts of the A band that abut the I bands are occupied by the both actin and myosin filaments (where they interdigitate as described above).

Myofibrils comprising a fine actin filament enclosed between a thick pair of myosin filaments slide past each other instigated by nerve impulses.

The H zone becomes smaller and smaller due to the increasing overlap of actin and myosin filaments, and the muscle shortens.

When a muscle contracts, the actin is pulled along myosin toward the center of the sarcomere until the actin and myosin filaments are completely overlapped.

It is composed of a globular head with both ATP and actin binding sites, and a long tail involved in its polymerization into myosin filaments.

Movement of the filaments over each other happens when the globular heads protruding from myosin filaments attach and interact with actin filaments to form crossbridges.

Muscle contraction results from an attachment-detachment cycle between the myosin heads extending from myosin filaments and the sites on actin filaments.

The overall process is initiated by an external signal, typically through an action potential stimulating the muscle, which contains specialized cells whose interiors are rich in actin and myosin filaments.

Actin and myosin filaments are linked by temporary cross-bridges, each myosin filament usually being surrounded by 6 actin filaments (Garamvolgyi, 1965; Hagopian, 1966).

Quite separately, he developed the mathematical equations for the operation of myosin "cross-bridges" that generate the sliding forces between actin and myosin filaments, which cause the contraction of skeletal muscles.

The myosin filaments would interdigitate between the actin filaments in opposite directions and help to push the platelet granules into the centre of the platelet for release into the surface-connected open canalicular system.

Length of the actin and myosin filaments (taken together as sarcomere length) affects force and velocity - longer sarcomeres have more cross-bridges and thus more force, but have a reduced range of shortening.

In the 1950s he was one of the first to use electron microscopy to establish the sliding filament model for muscle contraction, involving the sliding between actin filaments and myosin filaments in striated skeletal muscle.