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

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.