PROTEINS start life as linear amino acid sequences and end up as beautifully folded, active structures. Our laboratory focuses on recently discovered machinery that drives PROTEIN FOLDING in the cell. Two types of folding helpers are being studied, the catalysts responsible for disulfide bond formation and the HEAT SHOCK PROTEINS, which CHAPERONE protein folding. A multifaceted approach combining genetic, structural and biophysical tools is being used to generate a detailed picture about how these folding machines work