title: Spontaneous dimer states of the Aβ(21-30) decapeptide.
abstract: Constant temperature and replica-exchange molecular dynamics simulations of two Aβ21-30 decapeptides in explicit solvent reveal metastable dimer states that are abundant near physiological temperatures. As Alzheimer's disease is associated with the neurotoxic oligomers of amyloid β-protein, the formation of these dimers provides insight into oligomer assembly.
authors.affiliation: Department of Physics, Drexel University, 3141 Chestnut Street, Philadelphia, USA. ccruz@drexel.edu.
authors.forename: Micholas Dean
authors.initials: MD
authors.lastname: Smith
authors.forename: J
authors.initials: J
authors.lastname: Srinivasa Rao
authors.forename: Luis
authors.initials: L
authors.lastname: Cruz
mesh_terms: D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000648:ultrastructure*; D001665:Binding Sites; D003198:Computer Simulation; D019281:Dimerization; D008956:Models, Chemical; D056004:Molecular Dynamics Simulation; D010446:Peptide Fragments / Q000737:chemistry* / Q000648:ultrastructure*; D044367:Phase Transition; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C501831:amyloid beta-protein (21-30)