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Out-of-register parallel β-sheets and antiparallel β-sheets coexist in 150 kDa oligomers formed by Amyloid-β(1–42)
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 arra...
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| Gepubliceerd in: | J Mol Biol |
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| Hoofdauteurs: | , , , , , , , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2020
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7387221/ https://ncbi.nlm.nih.gov/pubmed/32470558 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2020.05.018 |
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