Metadynamics simulation of prion protein: beta-structure stability and the early stages of misfolding.

@article{Barducci2006MetadynamicsSO,
  title={Metadynamics simulation of prion protein: beta-structure stability and the early stages of misfolding.},
  author={Alessandro Barducci and Riccardo Chelli and Piero Procacci and Vincenzo Schettino and Francesco Luigi Gervasio and Michele Parrinello},
  journal={Journal of the American Chemical Society},
  year={2006},
  volume={128 8},
  pages={2705-10}
}
In the present study we have used molecular dynamics simulations to study the stability of the antiparallel beta-sheet in cellular mouse prion protein (PrP(C)) and in the D178N mutant. In particular, using the recently developed non-Markovian metadynamics method, we have evaluated the free energy as a function of a reaction coordinate related to the beta-sheet disruption/growth. We found that the antiparallel beta-sheet is significantly weaker in the pathogenic D178N mutant than in the wild… CONTINUE READING

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