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• W1985386364 abstract "The molecular conformation of silk fibrion is characterized by solid-state 13C NMR before spinning (silk I structure) and after spinning (silk II structure). We compare native silk fibers with the quasi-crystalline Cp-fraction and a synthetic model peptide (Ala-Gly)15, both of which can be converted either into silk I by dialysis from 9 M LiBr or into silk II by treatment with formic acid. Our results demonstrate that silk II fibers are intrinsically heterogeneous, consisting of beta-sheets, distorted beta-turns, and distorted beta-sheets. This higher-order heterogeneity is revealed by the 13C-NMR Cbeta-peak of Ala, indicating that the Ala side chains are stacked partially in parallel and partially face-to-face, at a ratio of 1:2." @default.
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• W1985386364 date "2002-07-01" @default.
• W1985386364 modified "2023-09-29" @default.
• W1985386364 title "Heterogeneous Structure of Silk Fibers from <i>Bombyx </i><i>m</i><i>ori </i>Resolved by ¹³C Solid-State NMR Spectroscopy" @default.
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• W1985386364 doi "https://doi.org/10.1021/ja020244e" @default.
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