Conformation coupled enzyme catalysis: Single-molecule and transient kinetics investigation of dihydrofolate reductase

Keyphrases

• Active Loop 16%
• Activity Flow 16%
• Amino Acid Position 16%
• Amino Acids 16%
• Being Observed 16%
• Catalytic Activity 33%
• Collective Information 16%
• Conformational Change 83%
• Conformational Transition 16%
• Coupled Catalysis 16%
• Coupled Enzymes 100%
• Cysteine 16%
• Distance Changes 16%
• Enzyme Catalysis 100%
• Equilibrium Mixtures 16%
• Flow Studies 16%
• Fluorescence Intensity 16%
• Fluorescence Quencher 16%
• Fluorescent Probe 16%
• Hydride Transfer 33%
• Isotope Effect 16%
• Kinetic Investigation 100%
• Methylenetetrahydrofolate Reductase (MTHFR) 100%
• Nicotinamide Adenine Dinucleotide Phosphate (NADPH) 16%
• Reverse Reaction 16%
• Single Molecule 16%
• Single-molecule Fluorescence Microscopy 16%
• Single-molecule Fluorescence Resonance Energy Transfer (smFRET) 33%
• Single-molecule Kinetics 100%
• Site-directed mutagenesis 16%
• Stopped Flow 16%
• Transient Kinetics 100%

Biochemistry, Genetics and Molecular Biology

• Active Site 16%
• Amino Acids 33%
• Conformation 100%
• Conformational Change 100%
• Cysteine 16%
• Dihydrofolate Reductase 100%
• Enzymatic Activity 33%
• Enzyme 16%
• Enzyme Catalysis 100%
• Fluorescence Microscopy 16%
• Fluorescence Resonance Energy Transfer 33%
• Fluorescent Probe 16%
• Kinetics 100%
• Lifespan 16%
• Site-Directed Mutagenesis 16%

Chemistry

• Amino Acid 33%
• Catalyst Activity 33%
• Conformational Transition 16%
• Cysteine 16%
• Dihydrofolates 100%
• Fluorescence Intensity 16%
• Fluorescence Microscopy 16%
• Fluorescence Quencher 16%
• Fluorescence Resonance Energy Transfer 33%
• Fluorescent Dye 16%
• Isotope Effect 16%
• NADPH 16%
• Rate Constant 33%
• Site-Directed Mutagenesis 16%
• Statistical Ensemble 33%