Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused

Protein Science

Volumn 8, Issue 8, 1999, Pages 1668-1674

  Kapust, Rachel B ^a   Waugh, David S ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Aggregation; Fusion protein; Glutathione S transferase; Inclusion bodies; Maltose binding protein; Protein folding; Solubility; Thioredoxin

Indexed keywords

GLUTATHIONE TRANSFERASE; MALTOSE BINDING PROTEIN; THIOREDOXIN;

ARTICLE; ESCHERICHIA COLI; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; SOLUBILITY;

ESCHERICHIA COLI;

EID: 0032787876     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.8.1668     Document Type: Article

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