Final answer:
ATP hydrolysis to ADP decreases the strength of binding between actin monomers in the filament, destabilizing the polymer and contributing to the dynamic state of actin filaments in cells.
Step-by-step explanation:
The hydrolysis of bound ATP to ADP in an actin filament decreases the strength of binding between monomers in the filament. This process destabilizes the actin polymer, leading to a dynamic state of polymerization and depolymerization. The actin monomers bound to ATP join the plus end of the actin polymer and, upon hydrolysis to ADP, reduce the binding strength of the monomers, promoting filament instability. The non-equilibrium dynamic nature of actin polymerization and depolymerization enables the cell's cytoskeleton to fulfill its various functions involving cell movement and shape change, with myosin playing a critical role in muscle contraction and cell motility. In contrast, the binding of myosin to actin filaments, in the presence of ATP, can lead to conformational changes that result in muscle contraction. It should be noted that the energy released by ATP hydrolysis can be used to modify the conformations of molecules like actin, impacting their interaction with other molecules.