Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins

Protein Science

Volumn 10, Issue 3, 2001, Pages 622-630

  Fox, Jeffrey D ^a   Kapust, Rachel B ^a   Waugh, David S ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Aggregation; Fusion protein; Inclusion bodies; Maltose binding protein; Protein folding; Solubility

Indexed keywords

CHAPERONE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CELL INCLUSION; ESCHERICHIA COLI; GENE MUTATION; HYDROPHOBICITY; LIGAND BINDING; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; ATP-BINDING CASSETTE TRANSPORTERS; BACTERIAL PROTEINS; CARRIER PROTEINS; ENZYME STABILITY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MOLECULAR CHAPERONES; MONOSACCHARIDE TRANSPORT PROTEINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SOLUBILITY; SURFACE PROPERTIES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0035104597     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.45201     Document Type: Article

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