Pivotal Role of Gly 121 in Dihydrofolate Reductase from Escherichia coli: The Altered Structure of A Mutant Enzyme May Form the Basis of Its Diminished Catalytic Performance

Biochemistry

Volumn 43, Issue 14, 2004, Pages 4119-4127

  Swanwick, Richard S ^a   Shrimpton, Paul J ^a   Allemann, Rudolf K ^a  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; COMPUTER SIMULATION; COUPLINGS; FLUORESCENCE; MELTING; MOLECULAR DYNAMICS; PROTEINS; SPECTROSCOPY; UREA;

MUTANTS; PROTEIN DYNAMICS;

ESCHERICHIA COLI;

BACTERIAL ENZYME; DIHYDROFOLATE REDUCTASE; GLYCINE; MUTANT PROTEIN; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; ENZYME INDUCTION; ENZYME MECHANISM; ENZYME RENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; HIGH TEMPERATURE; MELTING POINT; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; ROOM TEMPERATURE; SIMULATION;

CATALYSIS; CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; FREEZING; GLYCINE; HEAT; MUTAGENESIS, SITE-DIRECTED; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, FLUORESCENCE; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS; VALINE;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 1842531419     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036164k     Document Type: Article

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