Tertiary and Quaternary Structures of 0.19 α-Amylase Inhibitor from Wheat Kernel Determined by X-ray Analysis at 2.06 Å Resolution,-Reference-Cited by-同舟云学术

Tertiary and Quaternary Structures of 0.19 α-Amylase Inhibitor from Wheat Kernel Determined by X-ray Analysis at 2.06 Å Resolution,

Published:1997-11-01 Issue:44 Volume:36 Page:13503-13511
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Oda Yutaka¹,Matsunaga Takateru¹,Fukuyama Keiichi¹,Miyazaki Toshiyuki¹,Morimoto Toshihisa¹

Affiliation:

1. Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560, Japan, and Nisshin Flour Milling Co., Ltd., Koami-cho, Nihonbashi, Chuo-ku, Tokyo 103, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi971307m

Reference38 articles.

1. Buonocore, V., and Silano, V. (1986) inAdvances in Experimental Medicine and Biology(Friedman, M., Ed.) Vol. 199, pp 483−507, Plenum Press, New York.

2. Crystal structure determination, refinement and the molecular model of the α-amylase inhibitor Hoe-467A

3. The three-dimensional structure of the bifunctional proteinase k/α-amylase inhibitor from wheat (PKI3) at 2.5 Å resolution

4. Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat

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