Protein folding and thiol modification in the mammalian endoplasmic reticulum

The correct folding and assembly of proteins is the final stage in cellular protein synthesis. Protein folding requires a group of proteins that can either catalyse folding reactions or function as molecular chaperones to prevent non-productive protein aggregation. The lack of correct folding can lead to stress responses that ultimately cause diseases such as diabetes and cancer. Professor Bulleid will be investigating the molecular mechanisms that cells use to ensure that the chemical environment inside the endoplasmic reticulum enables the correct folding and assembly of secretory proteins. He will also study the regulation of protein folding by the modification of thiol chemical groups.