Prion protein amyloid: separation of scrapie infectivity from PrP polymers.

@article{Wille1996PrionPA,
  title={Prion protein amyloid: separation of scrapie infectivity from PrP polymers.},
  author={H. Wille and M. Baldwin and F. Cohen and S. DeArmond and S. Prusiner},
  journal={Ciba Foundation symposium},
  year={1996},
  volume={199},
  pages={
          181-99; discussion 199-201
        }
}
The prion protein (PrP) undergoes a profound conformational change when the cellular isoform (PrPc) is converted into the scrapie form (PrPSc). Limited proteolysis of PrPSc produces PrP27-30 which readily polymerizes into amyloid. To study the structure of PrP amyloid, we employed organic solvents that perturb protein conformation. 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP), which promotes alpha-helix formation, modified the ultrastructure of rod-shaped PrP amyloids, producing flattened ribbons… Expand
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