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Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils

Wild-type, full-length (40- and 42-residue) amyloid β-peptide (Aβ) fibrils have been shown by a variety of magnetic resonance techniques to contain cross-β structures in which the β-sheets have an in-register parallel supramolecular organization. In contrast, recent studies of fibrils formed in vitr...

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Autors principals: Qiang, Wei, Yau, Wai-Ming, Luo, Yongquan, Mattson, Mark P., Tycko, Robert
Format: Artigo
Idioma:Inglês
Publicat: National Academy of Sciences 2012
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Accés en línia:https://ncbi.nlm.nih.gov/pmc/articles/PMC3311365/
https://ncbi.nlm.nih.gov/pubmed/22403062
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1111305109
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