The interactions that shape amyloid fibrils in disease

Research output: Contribution to journalComment/debatepeer-review


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.

Original languageEnglish (US)
Pages (from-to)1045-1047
Number of pages3
Issue number8
StatePublished - Aug 4 2022

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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