Importance of a conserved phenylalanine-35 of cytochrome b5 to the protein's stability and redox potential

Protein Engineering

Volumn 10, Issue 5, 1997, Pages 575-581

  Yao, Ping ^a   Xie, Yi ^b   Wang, Yun Hua ^a   Sun, Yu Long ^a   Huang, Zhong Xian ^a   Xiao, Gu Tian ^a   Wang, Shun De ^a  

^a FUDAN UNIVERSITY   (China)

^b NONE

Author keywords

Cytochrome b5; Mutagenesis; Protein stability; Redox potential

Indexed keywords

CYTOCHROME B5; HEME; MUTANT PROTEIN; PHENYLALANINE; UREA;

AMINO ACID SEQUENCE; ARTICLE; AUTORADIOGRAPHY; CONTROLLED STUDY; GENE MUTATION; HYDROPHOBICITY; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CYTOCHROMES B5; ENZYME STABILITY; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PHENYLALANINE; PROTEIN DENATURATION; STRUCTURE-ACTIVITY RELATIONSHIP; UREA;

EID: 0030975015     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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