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. Author manuscript; available in PMC: 2014 Oct 3.
Published in final edited form as: J Phys Chem B. 2013 Sep 13;117(39):11518–11529. doi: 10.1021/jp405389n

Figure 1.

Figure 1

(A) Monomer conformations of the Osaka mutant (ΔE22) with different turns at Ser25-Ile30 (conformer 1) and Asp22-Gly28 (conformer 2), and (B) the wild type Aβ1–42 peptides with different turns at Ser26-Ile31 (conformer 1) and Asp23-Gly29 (conformer 2). Pore-lining residues are marked with blue callouts, and especially the Glu22 residues in the wild type Aβ1–42 peptides are marked with red callouts. In the peptide ribbon, hydrophobic, polar/Gly, positively charged, and negatively charged residues are colored white, green, blue, and red, respectively. Both termini of peptide are denoted as blue letter “N” for the N-terminus and red letter “C” for the C-terminus.