The role of an evolutionarily conserved cis-proline in the thioredoxin-like domain of human class Alpha glutathione transferase A1-1

Biochemical Journal

Volumn 372, Issue 1, 2003, Pages 241-246

  Nathaniel, Chris ^a   Wallace, Louise A ^b   Burke, Jonathan ^a   Dirr, Heini W ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

^b UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

Conformational stability; Glutathione; Thioredoxin fold

Indexed keywords

CATALYSIS; CONFORMATIONS; UREA;

THIOREDOXIN;

PROTEINS;

GLUTATHIONE TRANSFERASE; PROLINE; THIOREDOXIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; DISULFIDE BOND; ENDOPLASMIC RETICULUM; EVOLUTION; GENETIC CONSERVATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STABILITY;

GLUTATHIONE TRANSFERASE; GLYCINE; HUMANS; ISOENZYMES; KINETICS; MUTATION; PROLINE; PROTEIN DENATURATION; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; UREA;

EID: 0037954199     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021765     Document Type: Article

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