Nuclear magnetic resonance study of the role of M42 in the solution dynamics of escherichia coli dihydrofolate reductase

Biochemistry

Volumn 49, Issue 8, 2010, Pages 1606-1615

  Mauldin, Randall V ^a   Lee, Andrew L ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b University of North Carolina at Chapel Hill   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ALLOSTERIC MODULATORS; CATALYTIC CORE; CONFORMATIONAL DYNAMICS; CONFORMATIONAL FLUCTUATIONS; DIHYDROFOLATE REDUCTASE; DYNAMIC COMMUNICATION; HIGHER FREQUENCIES; LIGAND AFFINITY; LIGAND BINDING; METHYL GROUP; MULTIPLE TIME SCALE; MUTATIONAL EFFECTS; NONLOCAL SOURCE; NUCLEAR MAGNETIC RESONANCE STUDIES; PRODUCT RELEASE; PROTEIN DYNAMICS; SIDE-CHAIN; SIDE-CHAIN DYNAMICS; SOLUTION DYNAMICS; SUBDOMAIN; TIME-SCALES; WILD-TYPE ENZYMES;

AMIDES; CATALYSIS; ESCHERICHIA COLI; HYDROCARBONS; LIGANDS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; RESONANCE;

DYNAMICS;

DIHYDROFOLATE REDUCTASE; METHOTREXATE; METHYL GROUP; MUTANT PROTEIN;

ALLOSTERISM; ARTICLE; BINDING AFFINITY; CATALYSIS; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE MUTATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION;

ESCHERICHIA COLI PROTEINS; METHIONINE; METHOTREXATE; NADP; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; TETRAHYDROFOLATE DEHYDROGENASE; THERMODYNAMICS; TRYPTOPHAN;

ESCHERICHIA COLI;

EID: 77749322177     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901798g     Document Type: Article

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