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• W3032031494 abstract "We present solid-state NMR measurements of β-strand secondary structure and inter-strand organization within a 150-kDa oligomeric aggregate of the 42-residue variant of the Alzheimer's amyloid-β peptide (Aβ(1–42)). We build upon our previous report of a β-strand spanned by residues 30–42, which arranges into an antiparallel β-sheet. New results presented here indicate that there is a second β-strand formed by residues 11–24. Contrary to expectations, NMR data indicate that this second β-strand is organized into a parallel β-sheet despite the co-existence of an antiparallel β-sheet in the same structure. In addition, the in-register parallel β-sheet commonly observed for amyloid fibril structure does not apply to residues 11–24 in the 150-kDa oligomer. Rather, we present evidence for an inter-strand registry shift of three residues that likely alternate in direction between adjacent molecules along the β-sheet. We corroborated this unexpected scheme for β-strand organization using multiple two-dimensional NMR and 13C–13C dipolar recoupling experiments. Our findings indicate a previously unknown assembly pathway and inspire a suggestion as to why this aggregate does not grow to larger sizes." @default.
• W3032031494 created "2020-06-05" @default.
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• W3032031494 date "2020-07-01" @default.
• W3032031494 modified "2023-10-14" @default.
• W3032031494 title "Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1–42)" @default.
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• W3032031494 doi "https://doi.org/10.1016/j.jmb.2020.05.018" @default.
• W3032031494 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7387221" @default.
• W3032031494 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32470558" @default.
• W3032031494 hasPublicationYear "2020" @default.
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