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

Research paper by Yasumasa Fukushima

Indexed on: 01 Nov '00Published on: 01 Nov '00Published in: Polymer Bulletin



Abstract

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.