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When Troponin C binds calcium, it leads to a conformational change in the troponin-tropomyosin complex, which ultimately exposes the binding sites on actin for myosin. This process is a critical component of muscle contraction.

Calcium ions released during muscle activation bind to Troponin C, which is part of the troponin complex associated with the muscle filament. The binding of calcium induces a structural change that causes the troponin-tropomyosin complex to move away from the actin filament's myosin-binding sites. This exposure allows myosin heads to attach to actin, enabling the cross-bridge cycling essential for muscle contraction.

The other concepts presented in the options do not directly relate to the function of Troponin C in this context. For instance, blocking the myosin-binding site would prevent muscle contraction, contradicting the mechanism by which Troponin C facilitates contractions. While action potential generation is crucial for initiating the process of muscle contraction, it occurs prior to the calcium binding and does not involve Troponin C. Lastly, degradation of ATP does not occur as a direct result of calcium binding to Troponin C; rather, ATP is involved later in the muscle contraction cycle, specifically in