X-ray crystallography, CD and kinetic studies revealed the essence of the abnormal behaviors of the cytochrome b5 Phe35→Tyr mutant

European Journal of Biochemistry

Volumn 269, Issue 17, 2002, Pages 4287-4296

  Yao, Ping ^a   Wu, Jian ^b   Wang, Yun Hua ^a   Sun, Bing Yun ^a   Xia, Zong Xiang ^b   Huang, Zhong Xian ^a  

^a FUDAN UNIVERSITY   (China)

^b SHANGHAI INSTITUTE OF ORGANIC CHEMISTRY   (China)

Author keywords

Cytochrome b5; Folding; Mutagenesis; Stability; Structure

Indexed keywords

CYTOCHROME B5; HEME; HYDROXYL GROUP; MUTANT PROTEIN; PHENYLALANINE; TYROSINE;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISSOCIATION; ELECTRICITY; HEAT TREATMENT; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

ANIMALS; APOPROTEINS; BINDING SITES; CATTLE; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; CYTOCHROMES B5; ENZYME STABILITY; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MUTATION; MYOGLOBIN; OXIDATION-REDUCTION; PHENYLALANINE; PROTEIN DENATURATION; PROTEIN FOLDING; STRUCTURE-ACTIVITY RELATIONSHIP; TYROSINE;

EID: 0036042601     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03120.x     Document Type: Article

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