Stabilization mechanism of the tryptophan synthase α-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry

Journal of Biochemistry

Volumn 138, Issue 4, 2005, Pages 343-353

  Asada, Yukuhiko ^a   Sawano, Masahide ^a   Ogasahara, Kyoko ^b   Nakamura, Junji ^c   Ota, Motonori ^d   Kuroishi, Chizu ^a   Sugahara, Mitsuaki ^a   Yutani, Katsuhide ^a   Kunishima, Naoki ^a  

^a RIKEN HARIMA INSTITUTE   (Japan)

^b OSAKA UNIVERSITY   (Japan)

^c Tokyo Ryutsu Center   (Japan)

^d TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

Author keywords

DSC; Protein stability; Protein structure; Thermophile; Thermus thermophilus; Tryptophan synthase subunit; X ray analysis

Indexed keywords

TRYPTOPHAN SYNTHASE; TRYPTOPHAN SYNTHASE ALPHA; UNCLASSIFIED DRUG;

ARTICLE; BACTERIAL STRAIN; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; ENTHALPY; ENTROPY; ENZYME SUBUNIT; GENE DELETION; NONHUMAN; ORTHOLOGY; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE; PYROCOCCUS FURIOSUS; STRUCTURE ANALYSIS; THERMOPHILIC BACTERIUM; THERMOSTABILITY; THERMUS THERMOPHILUS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CALORIMETRY; CRYSTALLOGRAPHY, X-RAY; ENZYME STABILITY; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; TEMPERATURE; THERMUS THERMOPHILUS; TRYPTOPHAN SYNTHASE;

BACTERIA (MICROORGANISMS); PYROCOCCUS FURIOSUS; THERMUS THERMOPHILUS;

EID: 28244431804     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvi133     Document Type: Article

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