Stability of molecular order in silkworm silk

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

doi:10.1021/ma991223g

Stability of molecular order in silkworm silk

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

School of Engineering & Physical Sciences

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

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 language	English
Pages (from-to)	8671-8673
Number of pages	3
Journal	Macromolecules
Volume	32
Issue number	25
DOIs	https://doi.org/10.1021/ma991223g
Publication status	Published - 1999

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title = "Stability of molecular order in silkworm silk",

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.",

author = "Watt, {S. W.} and McEwen, {I. J.} and C. Viney",

year = "1999",

doi = "10.1021/ma991223g",

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T1 - Stability of molecular order in silkworm silk

AU - Watt, S. W.

AU - McEwen, I. J.

AU - Viney, C.

PY - 1999

Y1 - 1999

N2 - 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.

AB - 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.

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U2 - 10.1021/ma991223g

DO - 10.1021/ma991223g

M3 - Article

SN - 1520-5835

VL - 32

SP - 8671

EP - 8673

JO - Macromolecules

JF - Macromolecules

IS - 25

ER -

Stability of molecular order in silkworm silk

Abstract

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