The α-sheet: a missing-in-action secondary structure?
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Updated: Jun 4, 2026

Utilizing Time-Resolved Protein-Induced Fluorescence Enhancement to Identify Stable Local Conformations One α-Synuclein Monomer at a Time
Published on: May 30, 2021
Volodymyr Babin1, Christopher Roland, Celeste Sagui
1Center for High Performance Simulations, North Carolina State University, Raleigh, North Carolina 27695, USA.
Abstract:
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.
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