Influence of pH on the human prion protein: insights into the early steps of misfolding.

@article{Kamp2010InfluenceOP,
  title={Influence of pH on the human prion protein: insights into the early steps of misfolding.},
  author={Marc W van der Kamp and Valerie Daggett},
  journal={Biophysical journal},
  year={2010},
  volume={99 7},
  pages={2289-98}
}
Transmissible spongiform encephalopathies, or prion diseases, are caused by misfolding and aggregation of the prion protein PrP. Conversion from the normal cellular form (PrP(C)) or recombinant PrP (recPrP) to a misfolded form is pH-sensitive, in that misfolding and aggregation occur more readily at lower pH. To gain more insight into the influence of pH on the dynamics of PrP and its potential to misfold, we performed extensive molecular-dynamics simulations of the recombinant PrP protein… CONTINUE READING

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