Contribution of hydrogen bonds to the conformational stability of human lysozyme: Calorimetry and X-ray analysis of six tyrosine → phenylalanine mutants

Biochemistry

Volumn 37, Issue 26, 1998, Pages 9355-9362

  Yamagata, Yuriko ^a   Kubota, Masahiro ^a   Sumikawa, Yohei ^a   Funahashi, Jun ^a   Takano, Kazufumi ^a   Fujii, Satoshi ^a,b   Yutani, Katsuhide ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF SHIZUOKA   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

LYSOZYME; PHENYLALANINE; TYROSINE;

ARTICLE; BINDING SITE; CALORIMETRY; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; HUMAN; HUMAN CELL; HYDROGEN BOND; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN FOLDING;

CALORIMETRY, DIFFERENTIAL SCANNING; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; MURAMIDASE; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; TYROSINE;

EID: 0032581023     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi980431i     Document Type: Article

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