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Transmissible spongiform encephalopathies (TSEs), or prion diseases, are neurodegenerative disorders characterized by a spongiform neurodegeneration of the brain caused by prions [1,2].The pathogenic mechanisms of prion diseases are diverse, while the conformational conversion of the normal cellular prion protein (PrPc) into the scrapie isoform (PrPsc) is a central etiological event [3].To elucidate the structural stability and the unfolding dynamics of the animal prion protein, the temperature induced structural evolution of turtle prion protein (tPrPc) and bank vole prion protein (bvPrPc) have been performed with molecular dynamics (MD) simulation.