Methods for Studying Prion Protein Amyloid

Prion encephalopathies are neurodegenerative diseases characterized by the accumulation of abnormal isoforms of the prion protein (PrP) and the deposition of PrP amyloid in the central nervous systein (CNS) (1 , 2 ) The diseasespecific PrP molecules are distinguishable froin their normal homologs by their relative resistance to proteinase K digestion (1 , 2 ), they are thought to be derived from protease-sensitive precursors by a posttranslational process that involves a conformational change with a shift from α-helix to β-sheet structure (3 –5 )