title: Kinetic intermediates in amyloid assembly.
abstract: In contrast to an expected Ostwald-like ripening of amyloid assemblies, the nucleating core of the Dutch mutant of the Aβ peptide of Alzheimer's disease assembles through a series of conformational transitions. Structural characterization of the intermediate assemblies by isotope-edited IR and solid-state NMR reveals unexpected strand orientation intermediates and suggests new nucleation mechanisms in a progressive assembly pathway.
authors.affiliation: Departments of Chemistry and Biology, Emory University , Atlanta, Georgia 30322, United States.
authors.forename: Chen
authors.initials: C
authors.lastname: Liang
authors.forename: Rong
authors.initials: R
authors.lastname: Ni
authors.forename: Jillian E
authors.initials: JE
authors.lastname: Smith
authors.forename: W Seth
authors.initials: WS
authors.lastname: Childers
authors.forename: Anil K
authors.initials: AK
authors.lastname: Mehta
authors.forename: David G
authors.initials: DG
authors.lastname: Lynn
mesh_terms: D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D007700:Kinetics; D008958:Models, Molecular; D066329:Protein Aggregates; D017433:Protein Structure, Secondary
chemical_list: D016229:Amyloid beta-Peptides; D066329:Protein Aggregates