In this issue of Structure, van der Kant and colleagues use a computational approach to uncover what dictates assembly of proteins into amyloid fibrils. Structurally distinct amyloids have about 30% of their residues predisposed to cross-β conformation, while less favorable regions may be the source of polymorphism by interacting with stabilizing cofactors.
Copyright © 2022 Elsevier Ltd. All rights reserved.