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The availability of recombinant prion proteins (recPrP) has been exploited as a model system to study PrP-mediated toxicity, conversion and infectivity. It has been hypothesized that the central event in the pathogenesis of prion diseases is the conversion of PrP(C) to PrP (Sc). This involves a dramatic increase in beta sheet conformation as PrP(C) is converted to PrP(Sc) and it is widely believed that this conformational change affects the undefined function of PrP(C).