STRUCTURAL AND MECHANISTIC CONSEQUENCES OF POLYPEPTIDE BINDING BY GROEL

The remarkable ability of the chaperonin GroEL to recognise a diverse range of non-native states of proteins constitutes one of the most fas cinating molecular recognition events in protein chemistry. Recent str uctural studies have revealed a possible model for substrate binding b y GroEL and a high-resolution image of the GroEL-GroES folding machine ry has provided important new insights into our understanding of the m echanism of action of this chaperonin. Studies with a variety of model substrates reveal that the binding of substrate proteins to GroEL is not just a passive event, but can result in significant changes in the structure and stability of the bound polypeptide, the potential impac t of this on the mechanism of chaperonin-assisted folding is not fully understood, but provides exciting scope for further experiment.