newer information has begun to suggest that the hsp60 found in the mitochondria differs from that of the cytoplasm. with respect to the amino acid sequence, the cytoplasmic hsp60 has an n-terminal sequence not found in the mitochondrial protein. in gel electrophoresis analysis, significant differences were found in the migration of cytoplasmic and mitochondrial hsp60. the cytoplasmic hsp60 contains a signal sequence of 26 amino acids on the n terminus. this sequence is highly degenerate and is capable of folding into amphiphilic helix. antibodies against hsp60 targeted both the mitochondrial and cytoplasmic form. nonetheless, antibodies against the signal sequence targeted only the cytoplasmic form. under normal physiological condition, both are found in relatively equal concentrations. in times of stress or high need of hsp60 in either the cytoplasm or the mitochondria, the cell is capable for compensating by increasing the presence of hsp60 in one compartment and decreasing its concentration in the opposite compartment.