The focus of our research is to understand how proteins attain their correctly folded structure, within the cell, during and after their synthesis on ribosomes.
Successful protein folding in the cell requires the assistance of molecular chaperones.
Members of this diverse group of proteins can prevent protein aggregation, unfold kinetically trapped folding intermediates, dissolve aggregates, and promote folding of proteins to their native state. They are involved in intracellular protein transport, signal transduction and proteolysis. Many molecular chaperones are heat-shock proteins, reflecting the increased need for folding assistance in the cell under stress conditions. We are using a variety of techniques to analyze structure and function of several molecular chaperones. To address mechanistic aspects, we reconstitute chaperone-assisted protein folding in vitro with purified components.