The conversion of prion helix 1 from an α-helical into an extended conformation is generally
assumed to be an essential step in the conversion of the cellular isoform PrP C of the prion …

Revised Manuscript Received January 11, 1995® abstract: The structures of synthetic
peptides corresponding to regions of putative secondarystructure in the cellular prion protein …

A crucial step for transformation of the normal cellular isoform of the prion protein (PrPC) to
the infectious prion protein (PrPSc) is thought to entail a previously uncharacterized …

Background Prion diseases are fatal neurodegenerative disorders characterized by
misfolding and aggregation of the normal prion protein PrPC. Little is known about the …

The prion diseases are transmissible neurodegenerative disorders linked to a pathogenic
conformer (PrPSc) of the normal prion protein (PrPC). Accumulation of PrPSc occurs via a …

Prion propagation involves a conformational transition of the cellular form of prion protein
(PrP C) to a disease-specific isomer (PrP Sc), shifting from a predominantly α-helical …

Prion diseases are associated with the misfolding of the PrP (prion protein) from a largely α-
helical isoform to a β-sheet-rich oligomer. CD has shown that lowering the pH to 4 under …

A recombinant protein corresponding to the human prion protein domain encompassing
residues 90–231 (huPrP (90–231)) was expressed in Escherichia coli in a soluble form and …

Prion diseases are associated with a conformational switch in the prion protein (PrP) from its
normal cellular form (denoted PrPC) to a disease-associated “scrapie” form (PrPSc). A …

Conformational change in the prion protein (PrP) is thought to be responsible for a group of
rare but fatal neurodegenerative diseases of humans and other animals, including …