A topologically conserved aliphatic residue in α-helix 6 stabilizes the hydrophobic core in domain II of glutathione transferases and is a structural determinant for the unfolding pathway

Biochemical Journal

Volumn 336, Issue 2, 1998, Pages 413-418

  Wallace, Louise A ^a   Blatch, Gregory L ^a   Dirr, Heini W ^a  

^a UNIVERSITY OF THE WITWATERSRAND   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE; LEUCINE;

ALPHA HELIX; ARTICLE; DISSOCIATION; ENZYME KINETICS; FLUORESCENCE; GENETIC CONSERVATION; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STABILITY;

EID: 0032374057     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/bj3360413     Document Type: Article

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