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Biochemistry

Volumn 39, Issue 40, 2000, Pages 12336-12344

Equilibrium folding of dimeric class μ glutathione transferases involves a stable monomeric intermediate

(7) Hornby, J A T a Luo, J K a Stevens, J M a Wallace, L A a Kaplan, W a Armstrong, R N b Dirr, H W a

a UNIVERSITY OF THE WITWATERSRAND (South Africa)

b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE TRANSFERASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME DENATURATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY;

ANILINO NAPHTHALENESULFONATES; ANIMALS; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CROSS-LINKING REAGENTS; DIMERIZATION; ENZYME STABILITY; GLUTARAL; GLUTATHIONE TRANSFERASE; GUANIDINE; HEAT; ISOENZYMES; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; RATS; STRUCTURE-ACTIVITY RELATIONSHIP; UREA;

EID: 0034633885 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi000176d Document Type: Article

Times cited : (60)

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