Secondary structural analysis in the solid state for analogous sequential polypeptides of glycine-rich sequence of spider dragline silk

Summary

Four sequential copolypeptides poly(X-Gly-Gly) with X being Ala, Tyr, Gln, or Leu were prepared as a model of glycine-rich sequence of dragline spider silk produced by Nephila clavipes and their secondary structures in the solid state were characterized by FT-IR spectroscopy. Poly(Tyr-Gly-Gly), poly(Gln-Gly-Gly), and poly(Ala-Gly-Gly) form the β-sheet structures, whereas poly(Leu-Gly-Gly) existed as a disordered conformation as a cast film from formic acid. These results indicated that X-Gly-Gly sequences with Tyr, Gln, and Ala could contribute to the formation of the β-sheet structure in glycine-rich sequence.

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Received: 5 August 2000/Accepted: 24 August 2000

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Fukushima, Y. Secondary structural analysis in the solid state for analogous sequential polypeptides of glycine-rich sequence of spider dragline silk. Polymer Bulletin 45, 237–244 (2000). https://doi.org/10.1007/s002890070026

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Keywords

  • Spectroscopy
  • Solid State
  • Polypeptide
  • Secondary Structure
  • Formic Acid