Dr Peter Klappa joined the School of Biosciences in 1995.
It has been proposed that the incorrect folding of proteins is the molecular basis of various human diseases, e.g. cystic fibrosis, cancer and Alzheimer's disease. To understand disease-causing alterations in the folding pathway of proteins it is therefore important to investigate how proteins fold in general and why misfolding can occur.
Our interests are mainly focused on protein folding and the role molecular chaperones and folding catalysts play in this process. We are particularly interested in the structure, function and specificity of protein disulphide isomerases (protein folding catalysts that contain thioredoxin-like domains) and peptidyl proly cis-trans isomerases. The techniques we use include peptide synthesis, molecular biology, in-vitro transcription and in-vitro translation in cell free systems, cell culture, chemical cross-linking and immuno-histochemistry