The influence of Ser and Tyr residues on the structure of Bombyx Mori silk fibroin studied using high-resolution solid-state13C NMR spectroscopy and13C selectively labeled model peptides

Abstract

In order to examine the influence of Ser and Tyr residues in silk II structure of B. mori silk fibroin, we synthesized several 13C selectively labeled model peptides containing Ser and Tyr residues in (AG) n, mimicking the primary structure of B. mori silk fibroin. The 13C CP/MAS NMR spectra indicated that the presence of Ser residue promoted silk II structure, but Tyr residue destroyed silk II structure largely depending on the position of the introduction in the chain. © 2008 The Society of Polymer Science, Japan.