The focus of our laboratory

Disulfide bonds play critical roles in a range of cellular processes – from the stabilization of secreted proteins to regulating cellular adhesion and viral fusion.  Our multidisciplinary research program addresses how disulfides are generated and isomerized during oxidative protein folding in higher eukaryotes. We exploit a range of techniques including: peptide and protein purification, molecular biology, enzyme kinetics, rapid reaction studies, absorbance and fluorescence spectroscopy, NMR, mass spectrometry, and protein crystallography.

Current directions of our laboratory include:

A complete understanding of oxidative protein folding must combine insights from cell biology with a critical scrutiny of chemical feasibility and kinetic competence.

“Biology cannot ignore chemistry, much as I wish it could”

(John Maynard Smith)