Báo cáo khoa học: Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins
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Proteins are occasionally converted from their normal soluble state to highly ordered fibrillar aggregates (amyloids), which give rise to pathologi-cal conditions that range from neurodegenerative disorders to systemic amyloidoses. Recent methodological advances in solid-state NMR and EPR spectroscopy have enabled determination of the 3D structure of sev-eral amyloids at residue-level resolution.
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