Abstract
The chemical structure of silk fibroin, a fibrous biopolymer spun by the silkworm Bombyx mori (B.m.), contains three simple amino acids (glycine, alanine and serine), which represent about 85 mol% of the total amino acids. The fibroin chain is a block copolypeptide in which two basic polypeptide sequences (called “crystalline” and “amorphous” polypeptides) alternate regularly. The basic sequence of the crystalline polypeptide is of the -(Gly-Ala)n- type.
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References
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© 1999 Springer Science+Business Media Dordrecht
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Monti, P., Freddi, G., Tsukada, M., Bertoluzza, A., Asakura, T. (1999). Spectroscopic characterization of Bombyx mori silk fibroin: Raman spectrum of Silk I. In: Greve, J., Puppels, G.J., Otto, C. (eds) Spectroscopy of Biological Molecules: New Directions. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4479-7_38
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DOI: https://doi.org/10.1007/978-94-011-4479-7_38
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