Molecular Basis for Nonadditive Mutational Effects in Escherichia coli Dihydrofolate Reductase

Keyphrases

• Escherichia Coli Dihydrofolate Reductase 100%
• Mutational Effects 100%
• Side Chain 50%
• Additivity 50%
• Hydride Transfer 50%
• Oxidoreductase 25%
• Reaction Pathway 25%
• Methylenetetrahydrofolate Reductase (MTHFR) 25%
• Interaction Energy 25%
• Active Sites 25%
• Functional Groups 25%
• Catalytic Cycle 25%
• Free Energy 25%
• Substrate Binding 25%
• Free Energy Change 25%
• Cofactor Binding 25%
• NADP+ 25%
• Mutant Protein 25%
• Product Release 25%
• Energy Change 25%
• Substrate-binding Pocket 25%
• Non-additivity 25%
• Multiple Conformations 25%
• Enzyme Conformation 25%
• Enzyme Substrates 25%
• Related Sets 25%
• Ground-state Complex 25%
• Tetrahydrofolate 25%
• Synergistic Enhancement 25%
• Hydrophobic Substrates 25%
• Group Transformation 25%

Biochemistry, Genetics and Molecular Biology

• Escherichia coli 100%
• Dihydrofolate Reductase 100%
• Active Site 25%
• Conformation 25%
• Wild Type 25%
• Biochemistry 25%
• Enzyme 25%
• Enzyme Conformation 25%
• Oxidoreductase 25%
• Mutant Protein 25%
• Nicotinamide Adenine Dinucleotide Phosphate 25%
• Enzyme Substrate 25%
• Tetrahydrofolic Acid 25%

Chemistry

• Dihydrofolates 100%
• Free Energy 66%
• Ground State 33%
• NADP 33%
• Tetrahydrofolate 33%
• Cofactor 33%
• catalytic cycle 33%
• Tetrahydrofolic Acid 33%