Final answer:
The statement is true; myosin molecules have conserved head domains and highly variable tail domains, aligning with their roles in ATP hydrolysis, actin interaction and specific cellular functions.
Step-by-step explanation:
The statement that the head domains of various myosins are similar and the tail domains are highly divergent is true. Myosins are a large family of motor proteins that are involved in cell motility, muscle contraction, and intracellular transport. The myosin molecule consists of a head and a tail.
The head, which contains the site for ATP hydrolysis and the actin-binding site, is highly conserved across different myosins, reflecting the common fundamental tasks of ATP binding and hydrolysis, as well as interaction with actin filaments.
However, the tail region is variable and imparts specific functional roles to different myosin isoforms, allowing them to transport various cargoes and maintain their role in diverse cellular activities. Electron microscopy has provided visual evidence that myosin heads are flexible and can adopt different conformations necessary for muscle contraction.