Abstract
In an initial attempt to understand the structural organization of Bombyx mori silk fibroin stored in the silk gland using several solid-state NMR techniques, we recently reported the conformation of the crystalline form of silk I (The unprocessed conformation of the silk fibroin before spinning in the solid state) as a repeated type II β-turn structure (Ala, (φ,ψ) = (−60°,130°), and Gly, (φ,ψ ) = (70°,30°)) in a model peptide (Ala-Gly) 15 (Asakura et al. J. Mol. Biol. 2001, 306, 291−305). To examine the favorable secondary structure(s) associated with silk fibroin molecules, we analyzed the results of molecular dynamic (MD) simulations of three model dipeptides of the type Ac-Xxx-NHMe (where Xxx = Gly, Ala and Ser) in explicit water because the concentration of the silk fibroin before spinning in the middle silk gland is about 30% in water. The conformational probability maps constructed for these dipeptides indicate that the torsion angles of Gly, Ala, and Ser residues in the type II β-turn structure ar...
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