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

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 …

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 …

Prions are composed largely, if not entirely, of the scrapie isoform of the prion protein
(PrPsc). Conversion of the cellular isoform (PrPc) to PrPscis accompanied by a diminution in …

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 …

PrPSc is known to be the major, if not the only, component of the infectious prion. Limited
proteolysis of PrPSc produces an N-terminally truncated polypeptide of about 142 residues …

The major, and possibly only, component of the infectious prion is the scrapie prion protein
(PrPSc); the protease resistant core of PrPSc is PrP 27− 30, a protein of∼ 142 amino acids …

Prion diseases are a group of neurodegenerative disorders in humans and animals that
seem to result from a conformational change in the prion protein (PrP). Utilizing data …

Although no chemical modifications have been found to distinguish the cellular prion protein
PrPc from its infectious analogue PrPSc, spectroscopic methods such as Fourier transform …

Prion-related encephalopathies are characterized by cerebral accumulation of a post-
translationally modified form of the cellular prion protein (PrPC), designated PrPSc …