Final answer:
The domains in a subunit of HSP-60 are the ATPase, Co-chaperone, and Substrate Binding Domains. These domains play different roles in the protein folding process.
Step-by-step explanation:
The domains in a subunit of HSP-60 are the ATPase, Co-chaperone, and Substrate Binding Domains.
HSP-60 is a molecular chaperone involved in protein folding. It consists of multiple domains that play different roles in its function. The ATPase domain is responsible for ATP hydrolysis, which provides the energy needed for the chaperone activity. The co-chaperone domain aids in the proper folding of client proteins, while the substrate binding domain is where the client proteins bind to undergo folding.
Overall, the domains in a subunit of HSP-60 are crucial for its functioning as a molecular chaperone.