Figure 13.

(A) N-terminus (blue, 1–15), CHC (green, 16–21), loop (gray, 22–29), and C-terminus (purple, 30–40/42). (B) Schematic free energy landscape of Aβ monomers. Switching between some conformations occurs within 35 ns, as reported by FRET data.⁴²⁸ The conformation of S-shape N* from the fibril structure with PDB ID 2NAO was also sampled in CG simulations.⁴³⁷ (C) Representative structure of the Aβ42 tetramer, obtained by using multiscale MD simulation.⁴⁵¹ Blue and orange balls refer to the first and last residues, respectively, of monomer subunits. (D) Population of oligomer sizes obtained from simulations of 20-peptides.⁴⁶³