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Issue 7, 2007
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Correlation of the β-sheet crystal size in silk fibers with the protein amino acid sequence

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Abstract

Low voltage transmission electron microscopy (LVTEM) and wide angle X-ray scattering (WAXS) are used to independently determine the size of the β-sheet crystalline regions in Bombyx mori silk fibers. The peak in the size distributions of the major and minor axes of the anisotropic crystallites measured from the LVTEM images compare well with the average sizes as determined by Scherrer analysis of the X-ray fiber diagrams. These values are then discussed in the context of the B. mori fibroin heavy chain amino acid sequence, and the underlying mechanism for the organism's control on fiber crystallite size, and therefore mechanical properties, is proposed.

Graphical abstract: Correlation of the β-sheet crystal size in silk fibers with the protein amino acid sequence

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Supplementary files

Article information


Submitted
26 Jan 2007
Accepted
10 Apr 2007
First published
01 May 2007

Soft Matter, 2007,3, 877-882
Article type
Paper

Correlation of the β-sheet crystal size in silk fibers with the protein amino acid sequence

L. F. Drummy, B. L. Farmer and R. R. Naik, Soft Matter, 2007, 3, 877 DOI: 10.1039/B701220A

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