One of the fundamental unsolved problems in biology is how proteins attain their proper three dimensional conformation. Heat shock proteins and protein folding catalysts are vital in assisting proteins in this process. My laboratory is interested in understanding the molecular mechanism of these folding helpers. Understanding how the protein folding process is assisted is important to understand not just the vital protein folding itself, but also the numerous pathologies, like Alzheimer's, that result from defective protein folding.
We are using a multifaceted genetic, biophysical and structural approach to:
- Explore the Mechanism of Disulfide Bond Generation and isomerization.
- Investigate in vivo Folding Pathways.
- Experimentally evolve disulfide catalytic pathways
- Co-evolve protein folding catalysts and their substrates.
Another major project is to determine the function and 3D structure of newly identified heat shock proteins. This is complementary to our work on disulfide catalysis since many heat shock proteins chaperone protein folding.
