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Detailed structural studies of amyloid fibrils can elucidate the way in which their constituent polypeptides are folded and self-assemble, and exert their neurotoxic effects in Alzheimer's disease (AD). We have previously reported that when aqueous solutions of the N-terminal hydrophilic peptides of AD β-amyloid (Aβ) are gradually dried in a 2-Tesla magnetic field, they form highly oriented fibrils...