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• W2015504080 abstract "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-type PrP(C). The destabilization of PrP(C) beta-structure in the D178N mutant is correlated to the weakening of the hydrogen bonding network involving the mutated residue, Arg164 and Tyr128 side chains. This in turn indicates that such a network apparently provides a safety mechanism for the unzipping of the antiparallel beta-sheet in the PrP(C). We conclude that the antiparallel beta-sheet is likely to undergo disruption rather than growth under pathogenic conditions, in agreement with recent models of the misfolded monomer that assume a parallel beta-helix." @default.
• W2015504080 created "2016-06-24" @default.
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• W2015504080 date "2006-02-04" @default.
• W2015504080 modified "2023-09-26" @default.
• W2015504080 title "Metadynamics Simulation of Prion Protein: β-Structure Stability and the Early Stages of Misfolding" @default.
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• W2015504080 doi "https://doi.org/10.1021/ja057076l" @default.
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