The molecule that binds to myosin, which causes it to disconnect, is an ATP molecule
ATP
The power stroke of the cross bridge which binds ATP disconnecting it from the actin.
Actin changes shape.
The crossbridge cycle is the cyclical formation of links between actin and myosin. This results in the sliding of thin filaments towards the M line of a sarcomere. The myosin head undergoes conformation changes which allows it to swivel back and forth. In its low energy form, myosin has a low affinity for actin. The ATP prepares myosin for binding with actin by moving it to its high energy form position. When myosin contracts, it has a high affinity for actin.
cross bridge cycling ends when sufficient calcium has been actively transported back into the SR (to allow calcium to unbind from troponin)
The Gonhiqule depends on a molecule and cross the plasma membrane in an animal cell, but is a different story for the plant cell because of the cell wall.
shortening of the muscle fiber
The tropomyosin molecule blocks the active sites of the actin. Troponin is a molecule that is bound to the tropomyosin. Troponin needs CA+ (calcium ions) to bind to it in order to rotate the tropomyosin molecule and expose the actin molecules for the myosin heads to interact for muscle contraction.
The actin binding sites are exposed
Cross bridge
myosin binding to actin
What cross-bridge cycling requires is ATP, actin, inorganic phosphate, myosin, and ADP.
Cross bridge
The displacement of tropomyosin exposes the active sites of actin allowing cross bridge to form.
The power stroke of the cross bridge which binds ATP disconnecting it from the actin.
the pholsphorilation of ATP to ADP and an inorganic P
Energisation of the head takes place, then cross bridge linkage follows
Troponin controls the position of tropomyosin on the thin filament, enabling myosin heads to bind to the active sites on actin.