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  • Title: Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange.
    Author: Hoshino M, Katou H, Hagihara Y, Hasegawa K, Naiki H, Goto Y.
    Journal: Nat Struct Biol; 2002 May; 9(5):332-6. PubMed ID: 11967567.
    Abstract:
    Despite numerous efforts, the lack of detailed structural information on amyloid fibrils has hindered clarification of the mechanism of their formation. Here, we describe a novel procedure for characterizing the conformational flexibility of beta(2)-microglobulin amyloid fibrils at single-residue resolution that uses H/D exchange of amide protons combined with NMR analysis. The results indicate that most residues in the middle region of the molecule, including the loop regions in the native structure, form a rigid beta-sheet core, whereas the the N- and C-termini are excluded from this core. The extensively hydrogen-bonded beta-sheet core explains the remarkable rigidity and stability of amyloid fibrils. The present method could be used to obtain residue-specific conformational information of various amyloid fibrils, even though it does not provide a high resolution three-dimensional structure.
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