Slow Conformational Dynamics in the Hamster Prion Protein

Prions cause neurodegenerative diseases, such as scrapie in sheep, bovine spongiformencephalopathy (BSE) in cattle, Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker syndrome (GSS), fatal familial insomnia (FFI), kuru, and a new variant of CJD in humans. These diseases are associated with conversion of the normal cellular form of the prion protein (PrPC) to a pathogenic scrapie form (PrPSc), which is apparently the infectious agent in transmitted forms of the disease. The sequences of PrPSc and the noninfectious precursor PrPC are identical. Although both isoforms are chemically identical, they possess very different physicochemical properties. PrPC is substantially helical, but PrPSc has ~40% -sheet.

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