Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region.

@article{Cobb2014ConformationalSO,
  title={Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region.},
  author={Nathan Jeremy Cobb and Marcin Izydor Apostol and Shugui Chen and Vytautas Smirnovas and Witold K Surewicz},
  journal={The Journal of biological chemistry},
  year={2014},
  volume={289 5},
  pages={
          2643-50
        }
}
Mammalian prion strains are believed to arise from the propagation of distinct conformations of the misfolded prion protein PrP(Sc). One key operational parameter used to define differences between strains has been conformational stability of PrP(Sc) as defined by resistance to thermal and/or chemical denaturation. However, the structural basis of these stability differences is unknown. To bridge this gap, we have generated two strains of recombinant human prion protein amyloid fibrils that… CONTINUE READING
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