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The central glycine-glycine motif provides conformational flexibility potentially important for receptor interactions

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Structural insights into meningeal amyloid fibrils derived from AD brains reveals polymorphous copper loaded aggregates with the N-terminal histidines 1314 (responsible for canonical A-copper coordination) resting on the outer structure that surprisingly do not participate in the -sheet structure, indicating these metal binding regions likely do not participate in the copper-induced aggregation of A

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