The α-sheet: a missing-in-action secondary structure?

Proteins. 2011 Mar;79(3):937-46. doi: 10.1002/prot.22935. Epub 2011 Jan 3.


The α-sheet has been speculated to play a role as a toxic conformer in amyloid diseases. However, except for relatively short fragments, its detection has remained elusive. Here, we present molecular dynamics simulations that support the existence of the α-sheet as a stable, metastable, or long-lived secondary structure in polyglutamine and, to a lesser extent, in polyasparagine aggregates.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Molecular Dynamics Simulation
  • Peptides / chemistry
  • Protein Structure, Secondary*


  • Peptides
  • polyglutamine
  • polyasparagine