What role do chaperonins play in protein folding?

Chaperonins are specialized proteins that assist in the correct folding of other proteins, helping them achieve their functional three-dimensional structure. The correct folding of proteins is crucial for their functionality, as misfolded proteins can lead to aggregation and various diseases. Chaperonins often create a sheltered environment, allowing polypeptides to fold without the risk of aggregation that can occur in the cellular milieu. Within this environment, the polypeptides can interact with each other and undergo necessary conformational changes that lead to proper folding.

While chaperonins do not catalyze reactions, transport proteins, or degrade misfolded proteins, their primary function is to ensure that nascent or newly synthesized polypeptides can fold correctly into their active forms. This scaffolding function is critical in maintaining cellular protein homeostasis and preventing the detrimental effects associated with unfolded or misfolded proteins.