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The central event in the pathogenesis of prion protein (PrP) is a profound conformational change from its α-helical (PrP C ) to its β-sheet-rich isoform (PrP Sc ). Many single amino acid mutations of PrP are associated with familial prion diseases, such as D202N, E211Q, and Q217R mutations located at the third native α-helix of human PrP. In order to explore the underlying structural...
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