Myosin heads bind to actin molecules when the former has hydrolyzed ATP?

Although the exact molecular mechanism is unknown, in vitro studies suggest a model in which the cycle stars with myosin (in the absence of ATP) tightly bound to F actin. ATP binding disassociates myosin from F actin and its hydrolysis induces a conformational chain in myosin that displace the myosin head by about 10 nm. ADP and PI remain bound to myosin, which is said to be in the "cocked" position. The myosin head then rebinds to a new position on F actin resulting in Pi release. This release triggers the "power stroke", in which ADP is released and the myosin head returns to its initial conformation, thereby sliding the actin filament toward the M line.  = FALSE