Unique Inversion Events of Residues around the Backbone in the Turn Domain of β-Arches in Amylin Fibrils

Yoav Atsmon-Raz, Vered Wineman-Fisher, Michal Baram, Yifat Miller

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

Orientational inversion events of residues along the turn domains of amylin fibrils have been detected. This exceptional phenomenon has been observed in isolated amylin fibrils and in the cross-seeding amylin-Aβ and amylin-NAC fibrils. These new findings provide new avenues for detection of side chain flipping and side chain inversion events in turn domains and loops of various proteins.

Original languageEnglish
Pages (from-to)1209-1213
Number of pages5
JournalACS Chemical Neuroscience
Volume10
Issue number3
DOIs
StatePublished - 20 Mar 2019

Keywords

  • Amyloid
  • peptide-plane in proteins
  • polymorphism
  • self-assembly
  • structural interconversion

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