HSP60, also known as chaperonins (Cpn), is a family of heat shock proteins originally sorted by their 60kDa molecular mass. They prevent misfolding of proteins during stressful situations such as high heat, by assisting protein folding. HSP60 belong to a large class of molecules that assist protein folding, called molecular chaperones.
Structure of the bacterial chaperonin GroEL.
Prefoldin (GimC) is a superfamily of proteins used in protein folding complexes. It is classified as a heterohexameric molecular chaperone in both archaea and eukarya, including humans. A prefoldin molecule works as a transfer protein in conjunction with a molecule of chaperonin to form a chaperone complex and correctly fold other nascent proteins. One of prefoldin's main uses in eukarya is the formation of molecules of actin for use in the eukaryotic cytoskeleton.
This is the crystal structure of an archaeal prefoldin taken from the archaeon Methanobacterium thermoautotrophicum. The image was produced by Siegerts, R., Scheufler, C., Moarefi, I. using X-Ray diffraction. The heterohexameric protein complex contains two alpha subunits, and four beta subunits. (PDB: 1FXK)