The Folding and Stability of Human Alpha Class Glutathione Transferase A1-1 Depend on Distinct Roles of a Conserved N-capping Box and Hydrophobic Staple Motif

Journal of Biological Chemistry

Volumn 276, Issue 34, 2001, Pages 32177-32183

  Cocco, Roberta ^a   Stenberg, Gun ^b   Dragani, Beatrice ^a   Principe, Daniela Rossi ^a   Paludi, Domenico ^a   Mannervik, Bengt ^b   Aceto, Antonio ^a  

^a UNIVERSITY OF CHIETI   (Italy)

^b UPPSALA UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME KINETICS; HYDROPHOBICITY; MUTAGENESIS; NUCLEATION; PROTEINS;

ENZYME RESIDUES; MUTANTS;

BIOCHEMISTRY;

GLUTATHIONE TRANSFERASE; GLUTATHIONE S-TRANSFERASE ALPHA; GLUTATHIONE TRANSFERASE ALPHA; ISOENZYME;

ALPHA HELIX; ARTICLE; ENZYME ACTIVATION; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MUTATION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE DEPENDENCE; THERMOSTABILITY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; GENETICS; HUMAN; KINETICS; METABOLISM; NUCLEOTIDE SEQUENCE; PROTEIN CONFORMATION; PROTEIN MOTIF; SITE DIRECTED MUTAGENESIS;

ESCHERICHIA COLI;

AMINO ACID MOTIFS; CONSERVED SEQUENCE; ENZYME ACTIVATION; ENZYME STABILITY; GLUTATHIONE TRANSFERASE; HUMANS; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 0035943609     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M104057200     Document Type: Article

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