https://pages.htgaa.org/2026b/casian-veselin/final-project/index.htmlI. Abstract Prions are misfolded proteins that exhibit ‘infectious’-like behaviour and are the root cause for multiple prion protein associated neurodiseases: Creutzfeldt–Jakob Disease, Kuru (not exclusively in humans) and Scrapie and Bovine spongiform encephalopathy (BSE, mad-cow disease) characteristically affecting ovines and bovines respectively. In humans, the gene PrPC encodes for the premature version of the cellular prion protein (253-a.a. long) found within neuroglia and neurons, its function and role remain ambiguous and have not been described fully (or so it is believed). After post-translational modification in the endoplasmic reticulum, the precursor protein loses its N-terminal signal peptide (1-22) and C-terminal signal peptide (232-253) and carries on as a mature, functional PrPC surface glycoprotein that is 208-209 residues long. Faulty folding or interaction with other midfolded prion proteins can lead the native cellular variant of the protein to display a different structure and, thus, behaviour: resulting isoform is called PrPSc (scrapie-associated prion protein).Hugoen