| Abstract
| - The Aβ1−42 monomer structure was assessed with a 790 ns molecular dynamics (MD) simulation, and theresults were compared with the NMR experiment on Aβ10−35 and Aβ1−40. Previous theoretical work in amodel of the His13−His14 region of Aβ defined the possible Cu(II) binding geometries at this site (Raffa etal. J. Biol. Inorg. Chem.2005, 10, 887−902). MD simulations totalling almost 2 μs were also carried out onCu(II)/Aβ1−42 systems, using the ab initio structures as templates for the copper binding site. This workfinds that the copper-free Aβ1−42 system may stabilize after ∼350 ns into a collapsed coil conformation,and we find good agreement with some, but not all, of the structural features determined experimentally forthe Aβ10−35 and Aβ1−40 peptides. The results of the Cu(II)/Aβ1−42 systems are compared to the Cu(II)-free Aβ1−42 simulation.
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