Final answer:
Normal prion protein (PrP⁼) has a structure rich in alpha helices and binds copper, playing roles in cell signaling and memory formation. It is prone to misfolding into a disease-causing form, PrP⁼, which aggregates and causes neurodegenerative diseases. PrP⁼ itself does not cause protein misfolding or aggregation.
Step-by-step explanation:
Features of Normal Prion Protein (PrPC)
The normal prion protein, known as PrPC, is predominantly structured with alpha helices and is found in healthy brain tissues. Its precise functions are not fully understood, but it is known to bind copper and is important for cell signaling and possibly other functions such as memory formation and cellular processes. PrPC can, however, become misfolded due to a spontaneous event, particularly in the presence of a mutant form of the protein, or through exposure to already misfolded prions, such as PrPSc, which is the disease-causing form of the protein. When PrPC is misfolded into PrPSc, it adopts a structure rich in beta-pleated sheets, becomes resistant to proteolysis, and can cause the aggregation of more proteins, forming amyloid plaques associated with neurodegenerative disorders.
Contrary to its pathological counterpart, PrPC does not induce misfolding of other proteins and does not aggregate, thus playing its role in normal cellular functions without causing disease.