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Tightly winding structure of sequential model peptide for repeated helical region in Samia cynthia ricini silk fibroin studied with solid-state NMR

Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184–8588, Japan

Reprint requests to: Tetsuo Asakura, Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan; e-mail: asakura{at}cc.tuat.ac.jp; fax: 81-42-383-7733

There are many kinds of silks from silkworms and spiders with different structures and properties, and thus, silks are suitable to study the structure-property relationship of fibrous proteins. Silk fibroin from a wild silkworm, Samia cynthia ricini, mainly consists of the repeated similar sequences by about 100 times where there are alternative appearances of the polyalanine (Ala)_12–13 region and the Gly-rich region. In this paper, a sequential model peptide, GGAGGGYGGDGG(A)₁₂GGAGDGYGAG, which is a typical sequence of the silk fibroin, was synthesized, and the atomic-level conformations of Gly residues at the N- and C-terminal ends of the polyalanine region were determined as well as that of the central Ala residue using ¹³C 2D spin diffusion solid-state nuclear magnetic resonance (NMR) under off-magic angle spinning. In the model peptide with -helical conformation, the torsion angle of the central Ala residue, the 19th Ala, was determined to be (, ) = (-60°, -50°), which was a typical -helical structure, but the torsion angles of two Gly residues, the 12th and 25th Gly residues, which are located at the N- and C-terminal ends of the polyalanine region, were determined to be (,) = (-70°, -30°) and (,) = (-70°, -20°), respectively. Thus, it was observed that the turns at both ends of polyalanine with -helix conformation in the model peptide are tightly wound.

Keywords: Structure of Samia cynthia ricini silk fibroin; 2D spin diffusion NMR under off-magic angle spinning; -helix of polyalanine region; determination of torsion angles

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