Influence of the dimer interface on glutathione transferase structure and dynamics revealed by amide H/D exchange mass spectrometry

Biochemistry

Volumn 44, Issue 31, 2005, Pages 10605-10612

  Codreanu, Simona G ^a   Thompson, Lawrence C ^a   Hachey, David L ^a   Dirr, Heini W ^b   Armstrong, Richard N ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF THE WITWATERSRAND   (South Africa)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; CATALYST ACTIVITY; DIMERS; HYDROPHOBICITY; MASS SPECTROMETRY; MOLECULAR STRUCTURE; MUTAGENESIS; PROTEINS; SOLVENTS;

BINDING DOMAINS; DIMERIC PROTEINS; GLUTATHIONE (GSH); HYDROPHOBIC INTERACTIONS;

ENZYMES;

AMIDE; DIMER; GLUTATHIONE TRANSFERASE; SOLVENT;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; ENZYME STRUCTURE; ESCHERICHIA COLI; HYDROPHOBICITY; MAMMAL; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; STRUCTURE ANALYSIS;

AMIDES; DEUTERIUM EXCHANGE MEASUREMENT; DIMERIZATION; ENZYME STABILITY; GLUTATHIONE TRANSFERASE; HYDROPHOBICITY; KINETICS; LIGANDS; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

MAMMALIA;

EID: 23244467325     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050836k     Document Type: Article

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