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. Author manuscript; available in PMC: 2013 Jan 25.
Published in final edited form as: J Am Chem Soc. 2006 Mar 22;128(11):3540–3542. doi: 10.1021/ja055973j

Figure 1.

Figure 1

Metal binding sites predicted by the model of the Aβ(10–35) fibril. (a) The six-sheet laminated fibril with the backbone atoms shown. These fibrils are composed of β-strands, associating into β-sheet with hydrogen bond parallel to fibril long axis, while β-sheets laminate perpendicular to the fibril axis. The spacing between strands in the sheet and the mean distance between laminated sheets are ~5 and ~10 Å, respectively. (b) Potential zinc-binding site formed between two β-strands within a sheet, as viewed along the peptide backbones and perpendicular to the axis of fibril propagation. (c) Potential zinc-binding site formed between two strands of different sheets, as viewed down the axis of fibril propagation. Red, oxygen; blue, nitrogen; magenta, metal ion.