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- W2009046737 abstract "A critical event in Alzheimer's disease is the transition of Abeta peptides from their soluble forms into disease-associated beta-sheet-rich conformers. Structural analysis of a complete D-amino acid replacement set of Abeta(1-42) enabled us to localize in the full-length 42-mer peptide the region responsible for the conformational switch into a beta-sheet structure. Although NMR spectroscopy of trifluoroethanol-stabilized monomeric Abeta(1-42) delineated two separated helical domains, only the destabilization of helix I, comprising residues 11-24, caused a transition to a beta-sheet structure. This conformational alpha-to-beta switch was directly accompanied by an aggregation process leading to the formation of amyloid fibrils." @default.
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- W2009046737 date "2001-04-11" @default.
- W2009046737 modified "2023-10-02" @default.
- W2009046737 title "Study of the Conformational Transition of Aβ(1−42) Using <scp>d</scp>-Amino Acid Replacement Analogues" @default.
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- W2009046737 doi "https://doi.org/10.1021/bi002005e" @default.
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