Secondary structure of prion proteins in prion disease like Creutz feldt-Jakob disease (CJD) is
Beta sheets Prions are caused by human prion related protein (PrP) (a glycoprotein rich in a helix). PrP is endogenous to the host and in most people, the PrP protein folds normally leaving the person healthy. Rarely, a mutation in the PrP gene will allow the protein to be made incorrectly and it will fold incorrectly making a PrPsc prion. (Which is a Rlycoprotein rich in ,beta sheets). Remember PrP --> Made up of a helixo PrPse --> Made up of 13 shee Pathoeenesis of Prion's disease | Normal endogenous human protein (human prion related protein) (PrP) | It is a glycoprotein rich in a helix and it folds normally | Mutation in the PrP protein | Folds improperly and result in PrPsc protein (It is a glycoprotein rich in (sheets) | PrPsc comes in contact with PrP | PrP too will fold uncorrectly resulting in more PrPsc | Aggregation of PrPsc | Destruction of nervous tissue | Prion disease
Beta sheets
Beta bend
Beta turus
Alfa helix