文摘
Aggregation of amyloid ¦Â-proteins (A¦Â) plays a key role in the mechanism of molecular pathogenesis of Alzheimer¡¯s disease (AD). It is known that full-length A¦Â(1-42) is more prone to aggregation than A¦Â(1-40). We here search stable conformations of solvated A¦Â(1-42) monomer by replica exchange molecular dynamics simulations based on classical force fields, and the most stable conformation is determined from the total energies evaluated by the ab initio fragment molecular orbital (FMO) calculations. In addition, based on the FMO results, the amino acid residues of A¦Â(1-42) contributing to the stabilization of the monomer are highlighted.