Hyper-thermostability of CutA1 protein, with a denaturation temperature of nearly 150 °C

FEBS Letters

Volumn 580, Issue 17, 2006, Pages 4224-4230

  Tanaka, Tomoyuki ^a   Sawano, Masahide ^a   Ogasahara, Kyoko ^b   Sakaguchi, Yasushi ^c   Bagautdinov, Bagautdin ^a   Katoh, Etsuko ^d   Kuroishi, Chizu ^a   Shinkai, Akeo ^a   Yokoyama, Shigeyuki ^a,e,f   Yutani, Katsuhide ^a  

^a Harima Institute ^*  (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c Tokyo Ryutsu Center   (Japan)

^d NATIONAL INSTITUTE OF AGROBIOLOGICAL SCIENCES   (Japan)

^e RIKEN YOKOHAMA INSTITUTE   (Japan)

^f UNIVERSITY OF TOKYO   (Japan)

Author keywords

DSC; Heat denaturation; Hyperthermophile; Ion pairs; Protein stability; Protein structure

Indexed keywords

BACTERIAL PROTEIN; MONOMER; PROTEIN CUTA1; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL GROWTH; CRYSTAL STRUCTURE; DENATURATION; DIFFERENTIAL SCANNING CALORIMETRY; ESCHERICHIA COLI; ION PAIR EXTRACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE; PYROCOCCUS HORIKOSHII; TEMPERATURE DEPENDENCE; THERMOSTABILITY; THERMUS THERMOPHILUS;

ARCHAEAL PROTEINS; ESCHERICHIA COLI PROTEINS; HEAT; PROTEIN DENATURATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PYROCOCCUS HORIKOSHII; STRUCTURAL HOMOLOGY, PROTEIN; THERMUS THERMOPHILUS;

ESCHERICHIA COLI; PYROCOCCUS HORIKOSHII; THERMUS THERMOPHILUS;

EID: 33745851081     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.06.084     Document Type: Article

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