The Ability to Enhance the Solubility of Its Fusion Partners Is an Intrinsic Property of Maltose-Binding Protein but Their Folding Is Either Spontaneous or Chaperone-Mediated

PLoS ONE

Volumn 7, Issue 11, 2012, Pages

  Raran Kurussi, Sreejith ^a   Waugh, David S ^a  

^a FREDERICK NATIONAL LABORATORY FOR CANCER RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO TERMINAL TELOPEPTIDE; CHAPERONE; DIHYDROFOLATE REDUCTASE; DUAL SPECIFICITY PHOSPHATASE; DUAL SPECIFICITY PHOSPHATASE 14; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GREEN FLUORESCENT PROTEIN; HISTIDINE; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; PROTEINASE; TOBACCO ETCH VIRUS PROTEASE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ESCHERICHIA COLI; IN VITRO STUDY; NONHUMAN; PROTEIN AGGREGATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; PROTEIN REFOLDING; SOLUBILITY;

CHAPERONIN 10; CHAPERONIN 60; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GENE ORDER; MALTOSE-BINDING PROTEINS; MOLECULAR CHAPERONES; PROTEIN BINDING; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SOLUBILITY;

ESCHERICHIA COLI; TOBACCO ETCH VIRUS;

EID: 84869205433     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049589     Document Type: Article

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