All Comments by Torleif Hard
- Anti-parallel Universe—Rare Amyloid Peptides in Cylinders, Sheets
- α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation.
- Rationally designed turn promoting mutation in the amyloid-β peptide sequence stabilizes oligomers in solution.
- Prion propagation and toxicity in vivo occur in two distinct mechanistic phases.
- Ion mobility-mass spectrometry reveals a conformational conversion from random assembly to β-sheet in amyloid fibril formation.
- Amyloid beta-protein dimers rapidly form stable synaptotoxic protofibrils.
- Discriminating early stage A{beta}42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study.