Structure of Cytochrome c552 from a Moderate Thermophilic Bacterium, Hydrogenophilus thermoluteolus: Comparative Study on the Thermostability of Cytochrome c-Reference-Cited by-同舟云学术

Structure of Cytochrome c552 from a Moderate Thermophilic Bacterium, Hydrogenophilus thermoluteolus: Comparative Study on the Thermostability of Cytochrome c

Published:2006-04-20 Issue:19 Volume:45 Page:6115-6123
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Nakamura Shota¹,Ichiki Shin-ichi¹,Takashima Hiroyuki¹,Uchiyama Susumu¹,Hasegawa Jun¹,Kobayashi Yuji¹,Sambongi Yoshihiro¹,Ohkubo Tadayasu¹

Affiliation:

1. Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka 565-0871, Japan, Graduate School of Biosphere Science, Hiroshima University, Higashi-Hiroshima, Hiroshima 739-8528, Japan, Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan, Daiichi Pharmaceutical Co., Ltd., Edogawa-ku, Tokyo 134-8630, Japan, and Osaka University of Pharmaceutical Sciences, Takatsuki, Osaka 569-1094, Japan

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0520131

Reference39 articles.

1. Stability and stabilization of globular proteins in solution

2. Thermophilic prokaryotes have characteristic patterns of codon usage, amino acid composition and nucleotide content

3. PROTEIN FAMILIES AND THEIR EVOLUTION—A STRUCTURAL PERSPECTIVE

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