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Volumn 123, Issue 15, 2001, Pages 3418-3428
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Energetically most likely substrate and active-site protonation sites and pathways in the catalytic mechanism of dihydrofolate reductase
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Author keywords
[No Author keywords available]
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Indexed keywords
CARBOXYLATION;
CATALYSIS;
ENZYMES;
GEOMETRY;
IONIZATION;
PERMITTIVITY;
POLARIZATION;
PROTONATION;
REDUCTION;
ASPARTIC ACID;
CARBOXYLIC ACID DERIVATIVE;
DIHYDROFOLATE REDUCTASE;
DIHYDROFOLIC ACID;
OXYGEN;
PROTON;
ARTICLE;
CALCULATION;
CATALYSIS;
COMPLEX FORMATION;
CONTROLLED STUDY;
DIELECTRIC CONSTANT;
ENERGY;
ENZYME ACTIVE SITE;
ENZYME STABILITY;
ENZYME SUBSTRATE;
ESCHERICHIA COLI;
GEOMETRY;
HYDROGEN BOND;
MICHAELIS MENTEN KINETICS;
MOLECULAR MODEL;
NONHUMAN;
POLARIZATION;
PROTON TRANSPORT;
QUANTUM MECHANICS;
REACTION ANALYSIS;
REDUCTION;
SIMULATION;
X RAY ANALYSIS;
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EID: 84961978282
PISSN: 00027863
EISSN: None
Source Type: Journal
DOI: 10.1021/ja0038474 Document Type: Article |
Times cited : (58)
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References (58)
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