Reduced stability and enhanced surface hydrophobicity drive the binding of apo-aconitase with GroEL during chaperone assisted refolding

International Journal of Biochemistry and Cell Biology

Volumn 42, Issue 5, 2010, Pages 683-692

  Gupta, Parul ^a   Mishra, Saroj ^a   Chaudhuri, Tapan Kumar ^a,b  

^a Hauz Khas ^*  (India)

^b INDIAN INSTITUTE OF TECHNOLOGY DELHI   (India)

Author keywords

Aconitase unfolding; Apo aconitase; GroEL assisted folding; Holo aconitase; Metallo protein biosynthesis

Indexed keywords

ACONITATE HYDRATASE; CHAPERONE; CHAPERONIN; CITRIC ACID; FERROUS SULFATE; GUANIDINE; METALLOPROTEIN; TRYPTOPHAN;

ARTICLE; CITRIC ACID CYCLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME STABILITY; ESCHERICHIA COLI; HYDROPHOBICITY; IONIC STRENGTH; NONHUMAN; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN SYNTHESIS;

ACONITATE HYDRATASE; APOENZYMES; CHAPERONIN 60; CIRCULAR DICHROISM; FUNGAL PROTEINS; GUANIDINE; HOLOENZYMES; HYDROPHOBICITY; IRON-SULFUR PROTEINS; KINETICS; OSMOLAR CONCENTRATION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN; YEASTS;

EID: 77649187195     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.01.002     Document Type: Article

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