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Tetsuo Asakura

Researcher at Tokyo University of Agriculture and Technology

Publications -  437
Citations -  12637

Tetsuo Asakura is an academic researcher from Tokyo University of Agriculture and Technology. The author has contributed to research in topics: Fibroin & Bombyx mori. The author has an hindex of 56, co-authored 425 publications receiving 11671 citations. Previous affiliations of Tetsuo Asakura include University of Fukui & Dr Emilio B Espinosa Sr Memorial State College of Agriculture and Technology.

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Study of Protein Conformation and Orientation in Silkworm and Spider Silk Fibers Using Raman Microspectroscopy

TL;DR: It is shown that, for systems with uniaxial symmetry such as silk, it is possible to determine the order parameters P2 and P4 of the orientation distribution function from intensity ratios of polarized Raman spectra and the most probable distribution of orientation was calculated using the information entropy theory.
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Preparation of non-woven nanofibers of Bombyx mori silk, Samia cynthia ricini silk and recombinant hybrid silk with electrospinning method

TL;DR: In this article, a cross polarization/magic angle spinning NMR spectroscopy was used to monitor the structural change of silk fibroins together with the detection of the residual HFA during the process of the fiber formation.
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A repeated β-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

TL;DR: The structure of a crystalline form of Bombyx mori silk fibroin, commonly found before the spinning process (known as silk I), was proposed by combining data obtained from two-dimensional spin-diffusion nuclear magnetic resonance under off magic angle spinning, rotational-echo double-resonance (REDOR), previously reported X-ray diffraction analyses and 13C NMR chemical shifts.
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Heterogeneous structure of silk fibers from Bombyx mori resolved by 13C solid-state NMR spectroscopy.

TL;DR: This work compares native silk fibers with the quasi-crystalline Cp-fraction and a synthetic model peptide (Ala-Gly)15, both of which can be converted either into silk I by dialysis from 9 M LiBr or into silk II by treatment with formic acid, and demonstrates that silk II fibers are intrinsically heterogeneous.