Chaperone GroES

How does the GroEL-GroES complex function as a chaperone to assist protein folding Although several aspects of the mechanism are not clear, the main features of the functional cycle are known. The first step is the... 

It is generally believed that energy-independent chaperones are unable to allow refolding of non-native proteins. They bind to hydrophobic surfaces of denatured proteins to prevent aggregation and pass them to energy-dependent chaperones such as the DnaK or the GroE chaperone machines. 

Fig. 3. Modulation of the activity of HrcA a working model. It is assumed that HrcA repressor synthesized de novo or dissociated from its operator is present in an inactive form unable to interact with its operator. Through interaction with the GroE chaperone machine, inactive HrcA is converted into its active form...

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