Conformational change of the methionine 20 loop of Escherichia coli dihydrofolate reductase modulates pKa of the bound dihydrofolate

Protein Science

Volumn 16, Issue 6, 2007, Pages 1087-1100

  Khavrutskii, Ilja V ^a   Price, Daniel J ^a   Lee, Jinhyuk ^a   Brooks III, Charles L ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Conformational change; Dihydrofolate; Dihydrofolate reductase; Flexible loop; Free energy perturbation; Methionine; Molecular dynamics; NADP+; NADPH; pKa shift

Indexed keywords

DIHYDROFOLATE REDUCTASE; DIHYDROFOLIC ACID; METHIONINE; METHIONINE 20; NICOTINAMIDE; PTERIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME CONFORMATION; ESCHERICHIA COLI; MODULATION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTON TRANSPORT; SIMULATION;

BINDING SITES; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; FOLIC ACID; KINETICS; METHIONINE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; TETRAHYDROFOLATE DEHYDROGENASE;

ESCHERICHIA COLI;

EID: 34249823367     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062724307     Document Type: Article

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