PRNP and prion disease: We have conducted exhaustive PCA analyses on a large set of PrP globular structures, as well as several subsets representing particular species of interest (human and mouse), or groupings which hold biological significance (TSE susceptibility or non-susceptibility); from these analyses we identified five conformationally variable subdomains in PrP undergoing varying levels of correlated movements in all datasets, and which are thought to be significant for the PrP conformational conversion process that underlies prion disease.