Description
Hsp10 is a molecular chaperone that plays a role in protein folding under normal and stress conditions. It binds to Hsp60 in the presence of ATP causing a change in Hsp60 conformation and thus enclosing a protein substrate within this complex. ATP hydrolysis by chaperonin-60 destabilizes the Hsp10-Hsp60 complex allowing it to dissociate and release the protein substrate.
Recombinant Human GroES (Hsp10) produced in E. coli is a single, nonglycosylated polypeptide chain containing 102 amino acids with a molecular weight of 10kDa