Báo cáo khoa học: Mutagenesis of the central hydrophobic cluster in Ab42 Alzheimer’s peptide Side-chain properties correlate with aggregation propensities
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Protein misfolding and deposition underlie an increasing number of debili-tating human disorders. Alzheimer’s disease is pathologically characterized by the presence of numerous insoluble amyloid plaques in the brain, com-posed primarily of the 42 amino acid humanb-amyloid peptide (Ab42). Disease-linked mutations in Ab42 occur in or near a central hydrophobic cluster comprising residues 17–21.
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