We are investigating the contribution of PDI's domain structure to its function as a folding catalyst and molecular chaperone. In addition to its function as a folding catalyst, at in vivo concentrations PDI also behaves as a molecular chaperone, decreasing the aggregation of aggregation-prone proteins. PDI's anti-chaperone behavior may function to protect proteins against degradation. We are also using the concepts developed in the studies of the mechanism of molecular chaperones to develop new approaches to folding both in vitro and in genetically engineered strains of Escherichia coli. During the protein folding reaction, foldases accelerate slow chemical processes such as disulfide bond formation and proline isomerization that must accompany the formation of the correct, native structure.
Chaperones assist folding by preventing aggregation of the folding polypeptide.
Our research uses the techniques of molecular biology and biophysics to understand how foldases and chaperones assist the protein folding reaction. Sulfhydryl oxidase from egg white. A facile catalyst for disulfide bond formation in proteins and peptides, J. Biol. Contributions of Aspartate 49 and Phenylalanine 142 Residues of a Tight Binding Inhibitory Protein of beta-Lactamases J. Biol. In vivo and in vitro function of the Escherichia E. coli periplasmic cysteine oxidoreductase DsbG, J. Biol.