Stability of molecular order in silkworm silk

S. W. Watt, I. J. McEwen, C. Viney

Research output: Contribution to journalArticle

Abstract

DSC runs were performed on as-spun B. mori cocoon silk, and on silk that had been boiled in distilled water. To confirm the molecular as well as microstructural stability of silk fibroin subjected to boiling, ninhydrin was used to test for the absence of solubilized or degraded protein fragments in the boiling medium. The stability of the silk microstructure suggests that the crystalline fraction is connected by extended chains throughout the microstructure.

Original languageEnglish
Pages (from-to)8671-8673
Number of pages3
JournalMacromolecules
Volume32
Issue number25
DOIs
Publication statusPublished - 1999

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Bombyx
Silk
Fibroins
Ninhydrin
Morus
Water
Proteins

Cite this

Watt, S. W., McEwen, I. J., & Viney, C. (1999). Stability of molecular order in silkworm silk. Macromolecules, 32(25), 8671-8673. https://doi.org/10.1021/ma991223g
Watt, S. W. ; McEwen, I. J. ; Viney, C. / Stability of molecular order in silkworm silk. In: Macromolecules. 1999 ; Vol. 32, No. 25. pp. 8671-8673.
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Watt, SW, McEwen, IJ & Viney, C 1999, 'Stability of molecular order in silkworm silk', Macromolecules, vol. 32, no. 25, pp. 8671-8673. https://doi.org/10.1021/ma991223g

Stability of molecular order in silkworm silk. / Watt, S. W.; McEwen, I. J.; Viney, C.

In: Macromolecules, Vol. 32, No. 25, 1999, p. 8671-8673.

Research output: Contribution to journalArticle

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