Fluorescent intensity of a novel NADPH-binding protein of Vibrio vulnificus can be improved by directed evolution

Biochemical and Biophysical Research Communications

Volumn 322, Issue 1, 2004, Pages 303-309

  Chang, Chun Chin ^a   Chuang, Yin Ching ^b   Chang, Ming Chung ^a  

^a NATIONAL CHENG KUNG UNIVERSITY   (Taiwan)

^b CHI MEI MEDICAL CENTER   (Taiwan)

Author keywords

BfgV; Directed evolution; Fluorescence; Modeling; NADPH; Short chain dehydrogenase reductase superfamily; Vibrio vulnificus

Indexed keywords

BINDING PROTEIN; BLUE FLUORESCENT PROTEIN; MUTANT PROTEIN; PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CONTROLLED STUDY; DNA SHUFFLING; ESCHERICHIA COLI; FLUORESCENCE; MOLECULAR EVOLUTION; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; VIBRIO VULNIFICUS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; COMPUTER SIMULATION; DIRECTED MOLECULAR EVOLUTION; DNA SHUFFLING; LUMINESCENT PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NADP; PROTEIN CONFORMATION; PROTEIN ENGINEERING; RECOMBINANT FUSION PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; VIBRIO VULNIFICUS;

ESCHERICHIA COLI; VIBRIO; VIBRIO VULNIFICUS;

EID: 4143080269     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.07.117     Document Type: Article

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