What are the causes that makes the actin and myosin filaments to slide past one another during muscle contraction?

When calcium ions bind to troponin, causing conformational changes in troponin that allow tropomyosin to move away from the myosin binding sites on actin. Once the tropomyosin is removed, a cross-bridge can form between actin and myosin, causing contraction.

Explanation:

Muscles contract through the action of two proteins called actin and myosin.There are two other regulatory proteins tropomyosin and troponin. Muscles are composed of two major protein filaments: a thick filament composed of the protein myosin and a thin filament composed of the protein actin.Skeletal muscle is composed of a repeating structure of myosin and actin fibers. Each myosin thick filament is surrounded by actin thin filaments, and each thin filament is surrounded by thick filaments. Muscle contraction occurs when these filaments slide over one another in a series of repetitive events.

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. In other words, for a muscle cell to contract, the sarcomere must shorten. ATP is critical to prepare myosin for binding and to “recharge” the myosin. ATP first binds to myosin, moving it to a high-energy state. The ATP is hydrolyzed into ADP and inorganic phosphate (Pi) by the enzyme ATPase. The energy released during ATP hydrolysis changes the angle of the myosin head into a “cocked” position, ready to bind to actin if the sites are available. ADP and Pi remain attached; myosin is in its high energy configuration.The muscle contraction cycle is triggered by calcium ions binding to the protein complex troponin, exposing the active-binding sites on the actin. As soon as the actin-binding sites are uncovered, the high-energy myosin head bridges the gap, forming a cross-bridge. Once myosin binds to the actin, the Pi is released, and the myosin undergoes a conformational change to a lower energy state. As myosin expends the energy, it moves through the “power stroke,” pulling the actin filament toward the M-line. When the actin is pulled approximately 10 nm toward the M-line, the sarcomere shortens and the muscle contracts. At the end of the power stroke, the myosin is in a low-energy position.

After the power stroke, ADP is released, but the cross-bridge formed is still in place. ATP then binds to myosin, moving the myosin to its high-energy state, releasing the myosin head from the actin active site. ATP can then attach to myosin, which allows the cross-bridge cycle to start again; further muscle contraction can occur. Therefore, without ATP, muscles would remain in their contracted state, rather than their relaxed state.

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