Fig. 7
From: Baicalein inhibits amyloid beta42 aggregation through disruption of the Asp23-Lys28 salt bridge
Secondary structure information (DSSP) of the Aβ42 fibrils and conformations over 100 ns simulation time. (A) Aβ42 pentamer alone and (B) Aβ42 pentamer with bound BCN. In the snapshots, the secondary structures of Aβ42 are represented as follows: α-helix (purple), 310-helix (blue), extended-β (yellow), bridge-β (tan), turn (cyan), and random coil (white). BCN is depicted in red. For clarity, side chains of Aβ42, hydrogens, water molecules, and ions are omitted.
