The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: Structural characterization of proline-substitution sites for protein thermostabilization

Journal of Molecular Biology

Volumn 269, Issue 1, 1997, Pages 142-153

  Watanabe, Kunihiko ^a   Hata, Yasuo ^b   Kizaki, Hidekazu ^a   Katsube, Yukiteru ^c   Suzuki, Yuzuru ^a  

^a KYOTO PREFECTURAL UNIVERSITY   (Japan)

^b KYOTO UNIVERSITY   (Japan)

^c OSAKA UNIVERSITY   (Japan)

Author keywords

Oligo 1,6 glucosidase; Proline residue; Proline substitution; Thermostability; X ray structure

Indexed keywords

BACTERIAL ENZYME; OLIGO 1,6 GLUCOSIDASE; PROLINE;

ALPHA HELIX; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BACILLUS CEREUS; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION; THERMOSTABILITY;

BACILLUS CEREUS; BACTERIA (MICROORGANISMS);

EID: 0031591389     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1018     Document Type: Article

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