Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils
Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils
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Publisher
United States: National Academy of Sciences
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Language
English
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United States: National Academy of Sciences
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Contents
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 vitro by the Asp23-to-Asn mutant of 40-residue Aβ (D23...
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Full title
Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils
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TN_cdi_crossref_primary_10_1073_pnas_1111305109
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_crossref_primary_10_1073_pnas_1111305109
Other Identifiers
ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1111305109
