Résumé
Mutations in the prion protein (PrP) can cause spontaneous prion diseases in humans (Hu) and animals. In transgenic mice, mutations can determine the susceptibility to the infection of different prion strains. Some of these mutations also show a dominant-negative effect, thus halting the replication process by which wild type mouse (Mo) PrP is converted into Mo scrapie. Using all-atom molecular dynamics (MD) simulations, here we studied the structure of HuPrP, MoPrP, 10Hu/MoPrP chimeras, and 1 Mo/sheepPrP chimera in explicit solvent. Overall, approximate to 2s of MD were collected. Our findings suggest that the interactions between 1 helix and N-terminal of 3 helix are critical in prion propagation, whereas the 2-2 loop conformation plays a role in the dominant-negative effect. An animated Interactive 3D Complement (I3DC) is available in Proteopedia at .