The acidity of protein fusion partners predominantly determines the efficacy to improve the solubility of the target proteins expressed in Escherichia coli

Journal of Biotechnology

Volumn 129, Issue 3, 2007, Pages 373-382

  Su, Yu ^a   Zou, Zhurong ^a   Feng, Shuying ^a   Zhou, Pei ^a   Cao, Lijuan ^a  

^a EAST CHINA NORMAL UNIVERSITY   (China)

Author keywords

msyB; Protein acidity; Protein solubility enhancement; Solubility model of Wilkinson Harrison

Indexed keywords

MUTANTS; PROTEIN ACIDITY; PROTEIN FUSION; PROTEIN SOLUBILITY;

ENZYME KINETICS; ESCHERICHIA COLI; HYDROPHILICITY; MUTAGENESIS; PH EFFECTS; SOLUBILITY;

PROTEIN FOLDING;

AMINO ACID; BACTERIAL PROTEIN; CALMODULIN; ENTEROPEPTIDASE; HYBRID PROTEIN; PROTEIN MSYB; SUMO PROTEIN; THIOREDOXIN; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; ESCHERICHIA COLI; EVALUATION; HYDROPHILICITY; MOLECULAR MODEL; MOLECULAR SIZE; NONHUMAN; PARAMETER; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SOLUBILITY; WILKINSON HARRISON MODEL;

BIOTECHNOLOGY; COMPUTATIONAL BIOLOGY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENTEROPEPTIDASE; ESCHERICHIA COLI PROTEINS; GREEN FLUORESCENT PROTEINS; HYDROGEN-ION CONCENTRATION; MODELS, BIOLOGICAL; PROTEIN BINDING; RECOMBINANT FUSION PROTEINS; SOLUBILITY;

BOVINAE; ESCHERICHIA COLI;

EID: 34147140074     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.01.015     Document Type: Article

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