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The right answer is the force generated and duration of contraction would be greater than control. Thick myosin filaments and thin actin filaments glide past one another to cause muscle contraction.
Cross-bridges that protrude from myosin filaments and engage in periodic interactions with actin filaments when ATP is hydrolyzed are usually thought to be the driving force behind this mechanism. According to recent biochemical investigations, there are two primary conformations for the myosin cross-bridge. The cross-bridge binds to actin very strongly in one conformation that takes place in the absence of MgATP and detaches slowly in another. When every cross-bridge is connected in this manner, the muscle is rigid and incredibly stretch-resistant. The attachment of MgATP causes the second conformation to occur. The cross-bridge provides very little stretch resistance in this conformation because it binds to actin weakly and attaches and detaches so quickly that it can move from one actin site to another. Depolarization and calcium ion release, actin and myosin cross-bridge construction, actin and myosin filament sliding mechanism, and sarcomere shortening are some of the fundamental steps in the contraction of muscles (muscle contraction).
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