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Differentiating Folds of Prion and Doppel Proteins Through Stabilization Mechanisms

This study explores the distinct folding and stabilization mechanisms of Prion and Doppel proteins. The supplementary material includes graphs depicting the components of eigenvectors from simulations and their contributions to global energy, revealing negative peaks attributed to repulsive interactions. Additionally, it showcases RMSD superposition matrices for the first ten conformational clusters from 450K simulations, highlighting the clustering behaviors of these proteins at varying conditions (310K, 350K, and 450K). Understanding these elements is crucial for insights into prion diseases and protein misfolding.

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Differentiating Folds of Prion and Doppel Proteins Through Stabilization Mechanisms

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  1. Similar Folds with Different Stabilization Mechanisms: The Cases of Prion and Doppel Proteins S. Colacino, G. Tiana, G. Colombo Supplementary Material. Pages 2-7 Graphs showing the components of eigenvectors 2 and 3 from each simulation. Negative peaks appear showing the contribution of repulsive interactions to the global energy. Supplementary Material. Pages 8 RMSD superposition matrices of the structures of the first 10 conformational clusters from the 450K simulation. Negative peaks appear showing the contribution of repulsive interactions to the global energy.

  2. PrP 310K

  3. PrP 350K

  4. PrP 450K

  5. Dpl 310K

  6. Dpl 350K

  7. Dpl 450K

  8. Prion Doppel Cluster number Cluster number Cluster number Cluster number 0 1.4 0 1.4

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