An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells.
A key molecular event in prion diseases is the conversion of the prion protein (PrP) from its normal cellular form (PrPC) to the disease-specific form (PrPSc). The transition from PrPC to PrPSc involves a major conformational change, resulting in amorphous protein aggregates and fibrillar amyloid de...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2005
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