[HTML][HTML] Strain-dependent differences in β-sheet conformations of abnormal prion protein
Strain diversity in the transmissible spongiform encephalopathies (TSEs) has been
proposed to be determined by variations in the conformation of the abnormal, protease-
resistant form of prion protein (PrP-res). We have investigated whether infection of hamsters
with three TSE strains resulted in the formation of PrP-res with different conformations using
limited proteinase K (PK) digestion and infrared spectroscopy. PrP-res isolated from the
brains of hamsters infected with the hyper (HY), drowsy (DY), and 263K TSE strains yielded …
proposed to be determined by variations in the conformation of the abnormal, protease-
resistant form of prion protein (PrP-res). We have investigated whether infection of hamsters
with three TSE strains resulted in the formation of PrP-res with different conformations using
limited proteinase K (PK) digestion and infrared spectroscopy. PrP-res isolated from the
brains of hamsters infected with the hyper (HY), drowsy (DY), and 263K TSE strains yielded …