A review of the mechanism of protein refolding by GroEL-GroES machine is presented. Topics discussed include: chaperonins, specifically the establishment of a role on mediating protein folding in the cell; structural states of GroEL and the GroEL-GroES reaction cycle; and triggering productive folding. Under the second topic, focus is on the architecture of GroEL and GroES, polypeptide binding to a GroEL ring, and rigid body movements of GroEL during the reaction cycle. For the third topic, emphasis is on cis ternary complexes formation, GroEL-GroES formation, nature of the polypeptide load, and the polypeptide-GroEL-GroES-ADP complex as representative collision state.