Enhanced refolding of lysozyme with imidazolium-based room temperature ionic liquids: Effect of hydrophobicity and sulfur residue

Science China Chemistry

Volumn 55, Issue 8, 2012, Pages 1657-1662

  Bae, Sang Woo ^a   Chang, Woo Jin ^b   Koo, Yoon Mo ^a   Ha, Sung Ho ^c  

^a Inha University   (South Korea)

^b University of Wisconsin Milwaukee   (United States)

^c Hannam University   (South Korea)

Author keywords

Dilution refolding; Hydrophobicity; Lysozyme; Protein refolding; Room temperature ionic liquid; Sulfur

Indexed keywords

ACTIVE PROTEINS; ALKYL CHAIN; DILUTION METHOD; IMIDAZOLIUM CATION; IN-VITRO; INCLUSION BODIES; INTRAMOLECULAR DISULFIDE BONDS; MODEL PROTEINS; OPTIMUM CONCENTRATION; PROTEIN REFOLDING; REFOLDING; ROOM TEMPERATURE IONIC LIQUIDS; TETRAFLUOROBORATES;

COVALENT BONDS; DILUTION; HYDROPHOBICITY; IONIC LIQUIDS; POSITIVE IONS; RECOMBINANT PROTEINS; SULFUR;

ENZYMES;

EID: 84866175304     PISSN: 16747291     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11426-012-4678-7     Document Type: Article

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