The predicted secondary structures of the α/β-discordant segments of double Ala-substituted Aβ peptides and their native forms.

The secondary structure (upper row) for each amino acid residue was obtained by using the propensity-based prediction as described in Fig 2 caption of ref. 27. Adopting the notation used in Fig 2 caption of ref. 27, we denote the β-strands predicted with high and low probability by the symbols E and e, respectively. The symbols H and h were used for denoting the α-helical structures predicted with high and low probability, respectively.