Stability and unfolding of reduced Escherichia coli glutaredoxin 2: A monomeric structural homologue of the glutathione transferase family

Biochemistry

Volumn 47, Issue 40, 2008, Pages 10801-10808

  Gildenhuys, Samantha ^a   Wallace, Louise A ^a,b   Dirr, Heini W ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

^b GENENCOR INTERNATIONAL INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; ESCHERICHIA COLI; MOLECULAR INTERACTIONS; PORT TERMINALS; SYSTEM THEORY; UREA;

CONFORMATIONAL STABILITIES; DATA FITS; DIMERIC PROTEINS; GLUTAREDOXIN; GLUTAREDOXIN DOMAIN; GLUTATHIONE TRANSFERASE; HELICAL DOMAINS; MONOPHASIC; MONOTHIOL; N TERMINALS; ORTHOLOGS; QUATERNARY INTERACTIONS; SECONDARY STRUCTURES; TERTIARY STRUCTURES; TWO-STATE; U-MODEL; UNFOLDING KINETICS;

PROTEINS;

GLUTAREDOXIN; GLUTAREDOXIN 2; GLUTATHIONE TRANSFERASE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; DEGLUTATHIONYLATION; DENATURATION; ENZYME STRUCTURE; ESCHERICHIA COLI; ISOMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; REACTION ANALYSIS; SEQUENCE HOMOLOGY; SURFACE PROPERTY;

CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; GLUTAREDOXINS; GLUTATHIONE TRANSFERASE; KINETICS; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

ESCHERICHIA COLI;

EID: 53249109524     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801272t     Document Type: Article

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