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- W2044465982 abstract "Two synthetic peptide fragments of the plasma protein transthyretin (TTR), previously shown to form fibrillar structures in vitro, have been examined using electron microscopy and X-ray diffraction. The fibrils displayed all characteristics of cross β-sheet conformation with antiparallel strand spacing of 4.7 Å and intersheet spacings of 8 - 10 Å as well as reflections indicating further lateral repeating units. A third peptide containing a substitution equivalent to a mutation in TTR known to increase the propensity of TTR to form amyloid was also examined. It also formed fibrils and showed similar cross β-sheet structure, but with closer intersheet packing than its native equivalent." @default.
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- W2044465982 date "1993-05-01" @default.
- W2044465982 modified "2023-10-11" @default.
- W2044465982 title "X-Ray-Diffraction Studies of Fibrils Formed from Peptide Fragments of Transthyretin" @default.
- W2044465982 doi "https://doi.org/10.1006/bbrc.1993.1514" @default.
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