Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.

Abstract excerpt

BACKGROUND: Mutations in the cellular prion protein associated to familial prion disorders severely increase the likelihood of its misfolding into pathogenic conformers. Despite their postulation as incompatible elements with the native fold, these mutations rarely modify the native state structure. However they variably have impact on the thermodynamic stability and metabolism of PrP(C) and on the properties of...

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• Drug Design
• Methionine
• Molecular Dynamics Simulation
• Oxidation-Reduction
• Prion Diseases