What structural change do prions induce in proteins?

Prions are misfolded proteins that induce structural changes in normal proteins, particularly those that contain alpha-helices. The correct transformation prions facilitate is the conversion from an alpha-helical structure to a beta-pleated sheet conformation. This change is crucial because it alters the physical properties and functional characteristics of the affected proteins.

When the misfolded prion interacts with normal proteins, it promotes a conformational shift that favors beta-sheet structures over alpha-helices. This results in the aggregation of proteins into insoluble fibrils, which are associated with neurodegenerative diseases such as Creutzfeldt-Jakob Disease and Mad Cow Disease.

This misfolding and resultant aggregation disrupt normal cell function and lead to disease progression, which is why understanding the mechanism of prion action is critical in biochemistry and medicine.