The solubility and stability of recombinant proteins are increased by their fusion to NusA

Biochemical and Biophysical Research Communications

Volumn 322, Issue 3, 2004, Pages 766-771

  De Marco, Valeria ^a   Stier, Gunter ^a   Blandin, Stephanie ^a   De Marco, Ario ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

Escherichia coli; Expression vector; GST; NusA; Protein degradation; Recombinant protein

Indexed keywords

HYBRID PROTEIN; PROTEIN; PROTEIN NUSA; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; SOLUBILITY; STRUCTURE ANALYSIS;

DRUG STABILITY; ESCHERICHIA COLI PROTEINS; GENETIC VECTORS; GLUTATHIONE TRANSFERASE; KINETICS; OXIDATION-REDUCTION; PEPTIDE ELONGATION FACTORS; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS; SOLUBILITY; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; TOBACCO ETCH VIRUS; VECTORS;

EID: 4444378435     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.07.189     Document Type: Article

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