Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein.

@article{Wille2000ScrapieII,
  title={Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein.},
  author={H. Wille and S. Prusiner and F. Cohen},
  journal={Journal of structural biology},
  year={2000},
  volume={130 2-3},
  pages={
          323-38
        }
}
The prion protein undergoes a profound conformational change when the cellular isoform (PrP(C)) is converted into the disease-causing form (PrP(Sc)). Limited proteolysis of PrP(Sc) produces PrP 27-30, which readily polymerizes into amyloid. To study the relationship between PrP amyloid and infectivity, we employed organic solvents that perturb protein conformation. Hexafluoro-2-propanol (HFIP), which promotes alpha-helix formation, modified the ultrastructure of PrP amyloid and decreased the… Expand
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