Fluorescent intensity of a novel NADPH-binding protein of Vibrio vulnificus can be improved by directed evolution.
Chang, Chun Chin
Fluorescent intensity of a novel NADPH-binding protein of Vibrio vulnificus can be improved by directed evolution. [electronic resource] - Biochemical and biophysical research communications Sep 2004 - 303-9 p. digital
Publication Type: Comparative Study; Evaluation Study; Journal Article; Research Support, Non-U.S. Gov't
0006-291X
10.1016/j.bbrc.2004.07.117 doi
Amino Acid Sequence
Amino Acid Substitution
Computer Simulation
DNA Shuffling--methods
Directed Molecular Evolution--methods
Luminescent Proteins--chemistry
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed--genetics
NADP--genetics
Protein Conformation
Protein Engineering--methods
Recombinant Fusion Proteins--chemistry
Structure-Activity Relationship
Vibrio vulnificus--genetics
Fluorescent intensity of a novel NADPH-binding protein of Vibrio vulnificus can be improved by directed evolution. [electronic resource] - Biochemical and biophysical research communications Sep 2004 - 303-9 p. digital
Publication Type: Comparative Study; Evaluation Study; Journal Article; Research Support, Non-U.S. Gov't
0006-291X
10.1016/j.bbrc.2004.07.117 doi
Amino Acid Sequence
Amino Acid Substitution
Computer Simulation
DNA Shuffling--methods
Directed Molecular Evolution--methods
Luminescent Proteins--chemistry
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed--genetics
NADP--genetics
Protein Conformation
Protein Engineering--methods
Recombinant Fusion Proteins--chemistry
Structure-Activity Relationship
Vibrio vulnificus--genetics