Functional and kinetic analysis of the inter-domain communication network of the chaperonin GroEL

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A combination of circular permutation and stopped-flow fluorescence analysis was utilized to probe the relationship between the molecular mechanism of GroEL-facilitated protein folding and the unique three-domain subunit structure of the GroEL protein. Through analysis of multiple circularly permuted GroEL variants, we succeeded in correlating a specific, domain-dependent conformational change to an important functional aspect of the chaperonin mechanism. Additionally, our results prompt a reevaluation of the conventional mechanism of GroEL-facilitated folding.