Article
Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils.
Proceedings of the National Academy of Sciences of the United States of America - 20 Mar 2012
Qiang Wei, Yau Wai-Ming, Luo Yongquan, Mattson Mark P, Tycko Robert
Abstract excerpt
Wild-type, full-length (40- and 42-residue) amyloid β-peptide (Aβ) fibrils have been shown by a variety of magnetic resonance techniques to contain cross-β structures in which the β-sheets have an in-register parallel supramolecular organization. In contrast, recent studies of fibrils formed in vitro by the Asp23-to-Asn mutant of 40-residue Aβ (D23N-Aβ(1-40)), which is associated with early onset...
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