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Structural role of tyrosine in Bombyx mori silk fibroin, studied by solid-state NMR and molecular mechanics on a model peptide prepared as silk I and II by Tetsuo Asakura; Kohei Suita; Tsunenori Kameda; Sergii Afonin; Anne S. Ulrich is a Chemistry article available to read on EtoBox.
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## Abstract The influence of the bulky and H‐bonding Tyr side‐chain on its Ala‐ and Gly‐rich environment in __Bombyx mori__ silk fibroin was examined by ^13^C cross‐polarization magic angle spinning (CP/MAS), static ^2^H and ^19^F NMR and molecular mechanics calculations. Model peptides of the type (AG)~15~ were synthesized with Tyr in a number of different positions, precipitated under conditions favoring either of the two characteristic protein conformations, and the resulting structures were assigned from their ^13^C chemical shifts. Dialysis of native fibroin or the simple (AG)~15~ peptide from a 9 M LiBr solution against water produces silk I (the structure of silk before spinning), whereas drying from formic acid yields silk II (fibrous structure after spinning). We found that the introduction one or more Tyr into (AG)~15~ can have a dramatic effect not only on the local backbone conformation but also on the long‐range intermolecular chain packing in the samples. The antiparallel β‐sheet conformation of silk II is able readily to accommodate a single Tyr residue. Interestingly, the β‐turn conformation of silk I only remains stable when Tyr is positioned near the chain terminu
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- Author
- Tetsuo Asakura; Kohei Suita; Tsunenori Kameda; Sergii Afonin; Anne S. Ulrich
- Publisher
- John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; John Wiley and Sons Ltd; Wiley (ISSN 0749-1581)
- Published
- 2004
- Language
- EN
- Field
- Chemistry (Physical Sciences)