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Evidence from ¹³C solid-state NMR spectroscopy for a lamella structure in an alanine–glycine copolypeptide: A model for the crystalline domain of Bombyx mori silk fiber

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

(RECEIVED June 3, 2005; FINAL REVISION July 23, 2005; ACCEPTED July 25, 2005)

¹³C high-resolution solid-state NMR coupled with selective ¹³C isotope-labeling of different Ala one methyl carbons was used to clarify the structure of (AG)₁₅ peptide in the silk II structure as a model for the crystalline domain of Bombyx mori silk fiber. At the inner part of the peptide, the fraction of the peak at 16.6 ppm of the Ala C resonance assigned to -turn structure increased at 11th and 19th positions. These data indicate the appearance of the most probable lamellar structure having a turn structure at these two positions, although the position of turn was distributed along the chain.

Keywords: Bombyx mori silk; solid-state NMR; lamellar structure; (Ala-Gly)₁₅; stable isotope labeling peptide

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051525505.

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.

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