Summary of Research
The prion protein is central to the transmissible spongiform encephalopathies. During disease pathogenesis, the prion protein refolds from its normal cellular isoform (right) to an abnormal form composed of an increased amount of βsheet, Many details of this conversion, and of the normal function of the prion protein, remain unknown. The aim of the group is to understand how various features of prion protein biochemistry, including primary structure and modifications, secondary/tertiary structure and interactions with other molecules, contribute to both normal biology and to pathology during TSE infections. To do this we make use of a unique mixture of biophysical and biochemical techniques to probe molecular structure and interactions. Our research is based on spectroscopic investigations of primary and secondary protein structure and on in vitro misfolding assays. We make use of an extensive array of recombinant proteins also developed within the lab. Mass spectrometry is an important tool in our armoury, and we are also developing further proteomic technologies.