hsp60 possesses two main responsibilities with respect to mitochondrial protein transport. it functions to catalyze the folding of proteins destined for the matrix and maintains protein in an unfolded state for transport across the inner membrane of the mitochondria. many proteins are targeted for processing in the matrix of the mitochondria but then are quickly exported to other parts of the cell. the hydrophobic portion hsp60 is responsible for maintaining the unfolded conformation of the protein for transmembrane transport. studies have shown how hsp60 binds to incoming proteins and induces conformational and structural changes. subsequent changes in atp concentrations hydrolyze the bonds between the protein and hsp60 which signals the protein to exit the mitochondria. hsp60 is also capable of distinguishing between proteins designated for export and proteins destined to remain in the mitochondrial matrix by looking for an amphiphilic alpha-helix of 15-20 residues. the existence of this sequence signals that the protein is to be exported while the absence signals that the protein is to remain in the mitochondria. the precise mechanism is not yet entirely understood.