Final answer:
HSP-70 is a chaperone protein that folds proteins by hydrolyzing ATP to ADP, using the released energy to assist proteins in reaching their proper structure.
Step-by-step explanation:
HSP-70 is a type of chaperone protein involved in the folding of proteins. Its function is to ensure that proteins fold properly, thereby maintaining cellular functions. One of the critical aspects of HSP-70's function is its ability to utilize the energy derived from the hydrolysis of ATP. This process involves hydrolyzing ATP to ADP, which releases free energy that the HSP-70 uses to stabilize unfolded or partially folded proteins, preventing them from aggregating and assisting them in reaching their correct three-dimensional structures.
It is important to note that HSP-70's action is not associated with breaking peptide bonds or phosphodiester bonds nor does it have any activity involved with the binding to DNA or adding phosphates during its function. The correct answer to how HSP-70 fold proteins: A) By Hydrolyzing ATP.