Conformational changes in the active site loops of dihydrofolate reductase during the catalytic cycle

Keyphrases

• Conformational Change 100%
• Active Loop 100%
• Methylenetetrahydrofolate Reductase (MTHFR) 100%
• Catalytic Cycle 100%
• Loop Conformation 80%
• Active Sites 60%
• Nicotinamide Adenine Dinucleotide Phosphate (NADPH) 60%
• Folate 40%
• Binary Complexes 40%
• NADP+ 40%
• Kinetic Pathways 40%
• Protein Structure 20%
• NMR Techniques 20%
• Closed-loop 20%
• Functional Role 20%
• Conformational Transition 20%
• Substrate Binding 20%
• Occupancy 20%
• X-ray Crystallographic Analysis 20%
• Steady-state Conditions 20%
• Product Complexity 20%
• Multinuclear NMR 20%
• Holoenzyme 20%
• Flexible Loop 20%
• Conformational States 20%
• Pseudosubstrate 20%
• NMR Analysis 20%
• Nicotinamide 20%
• Ternary Complex 20%
• NMR Data 20%
• Apoenzyme 20%
• Cofactor-binding Site 20%
• Escherichia Coli Dihydrofolate Reductase 20%
• Substrate Binding Site 20%
• Cofactor Binding 20%
• Closed State 20%
• Unknown Structure 20%
• Tetrahydrofolate 20%
• Conformation in Solution 20%

Biochemistry, Genetics and Molecular Biology

• Active Site 100%
• Conformational Change 100%
• Dihydrofolate Reductase 100%
• Conformation 85%
• Solution and Solubility 28%
• Enzyme 28%
• Nicotinamide Adenine Dinucleotide Phosphate 28%
• Folic Acid 28%
• Alanine 28%
• Escherichia coli 14%
• Binding Site 14%
• Wild Type 14%
• Steady State 14%
• X Ray 14%
• Flexible Loop 14%
• Protein Structure 14%
• Ternary Complex 14%
• Tetrahydrofolic Acid 14%