A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH.

@article{Hornemann1998ASU,
  title={A scrapie-like unfolding intermediate of the prion protein domain PrP(121-231) induced by acidic pH.},
  author={Simone Hornemann and Rudi Glockshuber},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 11},
  pages={6010-4}
}
The infectious agent of transmissible spongiform encephalopathies is believed to consist of an oligomeric isoform, PrPSc, of the monomeric cellular prion protein, PrPC. The conversion of PrPC to PrPSc is characterized by a decrease in alpha-helical structure, an increase in beta-sheet content, and the formation of PrPSc amyloid. Whereas the N-terminal part of PrPC comprising residues 23-120 is flexibly disordered, its C-terminal part, PrP(121-231), forms a globular domain with three alpha… CONTINUE READING