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The α-helical C-terminal domain of full-length recombinant PrP converts to an in-register parallel β-sheet structure in PrP fibrils: Evidence from solid state NMR
We report the results of solid state nuclear magnetic (NMR) measurements on amyloid fibrils formed by the full-length prion protein PrP (residues 23-231, Syrian hamster sequence). Measurements of intermolecular (13)C-(13)C dipole-dipole couplings in selectively carbonyl-labeled samples indicate that...
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| 主要な著者: | , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2010
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3025268/ https://ncbi.nlm.nih.gov/pubmed/20925423 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi1013134 |
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