Kohei Komatsu

A Lamellar Structure in Alanine-Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form.

A. Naito, T. Asakura, H. Kaji, 2020, Biomacromolecules.

A repeated beta-turn structure in poly(Ala-Gly) as a model for silk I of Bombyx mori silk fibroin studied with two-dimensional spin-diffusion NMR under off magic angle spinning and rotational echo double resonance.

T. Yamane, K. Ohgo, T. Asakura, 2001, Journal of molecular biology.

Refinement of Repeated β-turn Structure for Silk I Conformation of Bombyx mori Silk Fibroin Using 13C Solid-State NMR and X-ray Diffraction Methods

K. Okuyama, K. Ohgo, T. Asakura, 2005 .

Determination of the torsion angles of alanine and glycine residues of model compounds of spider silk (AGG)10 using solid-state NMR methods

K. Ohgo, T. Asakura, J. Ashida, 2003, Journal of biomolecular NMR.