Misfolding pathways of the prion protein probed by molecular dynamics simulations.

@article{Barducci2005MisfoldingPO,
  title={Misfolding pathways of the prion protein probed by molecular dynamics simulations.},
  author={Alessandro Barducci and Riccardo Chelli and Piero Procacci and Vincenzo Schettino},
  journal={Biophysical journal},
  year={2005},
  volume={88 2},
  pages={1334-43}
}
Although the cellular monomeric form of the benign prion protein is now well characterized, a model for the monomer of the misfolded conformation (PrP(Sc)) remains elusive. PrP(Sc) quickly aggregates into highly insoluble fibrils making experimental structural characterization very difficult. The tendency to aggregation of PrP(Sc) in aqueous solution implies that the monomer fold must be hydrophobic. Here, by using molecular dynamics simulations, we have studied the cellular mouse prion protein… CONTINUE READING