Chaperonins are large double-ring complexes that provide a nano-compartment for single protein molecules to fold in isolation, unimpaired by aggregation.  A major focus of the group continues to be the mechanistic analysis of chaperonin-assisted protein folding using biophysical and biochemical methods. While many aspects of the chaperonin ATP-dependent mechanism have been unravelled in the past ten years, it remains unclear how protein folding inside the chaperonin nano-cage differs from spontaneous folding in bulk solution in terms of the pathways and energetics of the folding reactions. We are addressing these questions using the chaperonin system of E. coli, GroEL and GroES, as our main model.

            A more recent interest concerns the mechanism of chaperone-assisted protein assembly, i.e. the organization of folded subunits into complex oligomeric structures.  In this project we are using the assembly of hexadecameric Ribulose-bisphosphate carboxylase-oxygenase (Rubisco) as a paradigm.