8 – Misfolded proteins
2012
:
Structural analysis of properly folded proteins provides insight into their folding process and the origins of their biological properties; however, an equally rich trove of information presents itself in the form of misfolded proteins, particularly amyloidogenic ones. Such proteins exhibit structural modifications that induce the formation of large-scale fibrillary aggregates. Changes that promote amyloidogenesis also destroy the protein’s intended biological activity. Relating the phenomenon of amyloid generation to the proposed folding model suggests the importance of F-type motifs, emerging as a result of structural forms introduced by external forces.
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