Figure 8From: Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone proteinHypothetical model for peptide-1 fibril formation based on a molecular dynamics simulation. (A) Initial structure with two units of peptide-1 arranged in a β-antiparallel disposition. An intermolecular distance of 4 Å within the complementary charged amino acid residues (between the charged atoms) was used. (B). Snapshot representative of the final part of the simulation where the energy of the system was stabilized. (Blue: hydrophobic residues, green: acidic residues; magenta: basic residues).Back to article page