Cross-bridge
The release of ADP and P from the myosin heads causes the myosin heads to change shape.
globular heads
myosin crossbridge binding
During contraction, there are always some myosin heads attached to the actin myofilament when other myosin heads are detaching.
Binding of the myosin heads sequentially prevents the actin-binding sites on the thin filaments from becoming continuously occupied by myosin heads, allowing for the muscle fiber to relax and the sarcomere to lengthen.
Myosin heads contain ATPase enzymes, which hydrolyze ATP to provide energy for muscle contraction. This energy is used to power the movement of myosin heads along actin filaments during the sliding filament theory of muscle contraction.
myosin
Actin is the molecule that has a binding site for myosin heads. This interaction is crucial for muscle contraction as myosin binds to actin and generates force to cause muscle movement.
ATP allows actin and myosin filaments to release from each other during muscle contraction by assisting in the detachment of the myosin heads from actin. It also helps in resetting the myosin heads for the next contraction cycle by providing energy for the process of cross-bridge formation.
Cross bridge
No, the heads of myosin molecules do not contact the actin filaments when a muscle is relaxed. In a relaxed state, the binding sites on actin are blocked by tropomyosin, preventing myosin heads from attaching. When calcium ions are released during muscle contraction, they bind to troponin, causing a conformational change that moves tropomyosin and exposes the binding sites for myosin, allowing contraction to occur.
ATP is used to detach myosin heads and move them back to position for another "power stroke."