Analysis of ATP binding to CheA containing tryptophan substitutions near the active site

Biochemistry

Volumn 44, Issue 11, 2005, Pages 4375-4385

  Stewart, Richard C ^a  

^a UNIVERSITY OF MARYLAND   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; COMPLEXATION; CONFORMATIONS; CRYSTAL STRUCTURE; EMISSION SPECTROSCOPY; ESCHERICHIA COLI; FLUORESCENCE; PROTEINS; SUBSTRATES; X RAY ANALYSIS;

CHEMOTAXIS; NUCLEOTIDES; SIGNAL TRANSDUCTION; X RAY CRYSTAL STRUCTURE;

ADENOSINETRIPHOSPHATE;

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DERIVATIVE; CALCIUM; CHEA KINASE; MAGNESIUM; PHENYLALANINE; PROTEIN HISTIDINE KINASE; TRYPTOPHAN;

AMINO ACID SUBSTITUTION; ARTICLE; AUTOPHOSPHORYLATION; BINDING KINETICS; CHEMOTAXIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME PHOSPHORYLATION; ESCHERICHIA COLI; FLUORESCENCE; NONHUMAN; PRIORITY JOURNAL; SIGNAL TRANSDUCTION;

ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CALCIUM; CATIONS, DIVALENT; CHEMOTAXIS; ESCHERICHIA COLI; MAGNESIUM; MANGANESE; MEMBRANE PROTEINS; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN KINASES; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRYPTOPHAN;

EID: 15544364345     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0476026     Document Type: Article

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