Hydrogen-Bonding Structure of Serine Side Chains in Bombyx mori and Samia cynthia ricini Silk Fibroin Determined by Solid-State 2H NMR-Reference-Cited by-同舟云学术

Hydrogen-Bonding Structure of Serine Side Chains in Bombyx mori and Samia cynthia ricini Silk Fibroin Determined by Solid-State 2H NMR

Published:1999-09-15 Issue:21 Volume:32 Page:7166-7171
ISSN:0024-9297
Container-title:Macromolecules
language:en
Short-container-title:Macromolecules

Author:

Kameda Tsunenori¹,Ohkawa Yohei¹,Yoshizawa Keiko¹,Naito Junko¹,Ulrich Anne S.¹,Asakura Tetsuo¹

Affiliation:

1. Department of Biotechnology, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184, Japan, and Institut für Molekularbiologie, Friedrich-Schiller-Universität Jena, Winzerlaer Strasse 10, 07745 Jena, Germany

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Inorganic Chemistry,Polymers and Plastics,Organic Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ma990554q

Reference40 articles.

1. Asakura, T.; Kaplan, D. L. InEncyclopedia of Agricultural Science; C. J., Arutzen, Ed.; Academic Press: London, 1994; Vol. 4, pp 1−11.

2. Highly repetitive structure and its organization of the silk fibroin gene

3. Preferential codon usage and two types of repetitive motifs in the fibroin gene of the Chinese oak silkworm, Antheraea pernyi

4. The amino-terminal sequence of silk fibroin peptide Cp — A reinvestigation

5. An investigation of the structure of silk fibroin

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