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There are 15 genes in the human genome that encode proteins termed chaperonins with the HSPE1 encoded protein (chaperonin 10/Hsp10) being required as a co-chaperone for Hsp60 function.

Human Hsp60 was originally characterized as a mitochondrial chaperone involved in correct folding of mitochondrial proteins during their import into this organelle.

In addition, there is the small heat shock protein family often referred to as the Hsp25 family or the HSPB family.Proteins that are classified as chaperonins are large (800-900 k Da) double-ring complexes that function by globally enclosing substrate proteins for folding.Proteins up to a size of around 60 k Da can be acted upon by the chaperonins.Improper folding and protein aggregation can lead to the formation of potentially toxic species.To reduce and prevent these negative outcomes, cells harbor a complex network of molecular chaperones whose functions are to promote efficient folding and to prevent protein aggregation.