Mechanism of the conformational transitions in 6-hydroxymethyl-7,8- dihydropterin pyrophosphokinase as revealed by NMR spectroscopy

Keyphrases

• NMR Spectroscopy 100%
• Conformational Transition 100%
• Hydroxymethyl 100%
• Binary Complexes 100%
• Ternary Complex 75%
• Conformational Change 50%
• NMR Signal 50%
• Triphosphate 50%
• Cross Peak 50%
• Enzymatic Catalysis 50%
• Multiple Conformations 50%
• Antimicrobial 25%
• Folate 25%
• Protein Dynamics 25%
• Binding Affinity 25%
• Catalytic Cycle 25%
• Dimethyl 25%
• MgATP 25%
• Slow Exchange 25%
• NMR Solution Structure 25%
• Pyrophosphate 25%
• Catalytic Mechanism 25%
• Substrate Complexity 25%
• Conformational Properties 25%
• Multiple Sets 25%
• Binary Substrate 25%
• Catalytic Loop 25%

Biochemistry, Genetics and Molecular Biology

• Nuclear Magnetic Resonance Spectroscopy 100%
• Conformation 100%
• Conformational Change 100%
• Phosphotransferase 100%
• Kinase 100%
• Ternary Complex 60%
• Adenosine Triphosphate 40%
• Anabolism 20%
• Catalytic Mechanism 20%
• Solution Structure 20%
• Enzyme 20%
• Binding Affinity 20%
• Pyrophosphate 20%
• Folic Acid 20%
• Protein Dynamics 20%

Chemistry

• NMR Spectroscopy 100%
• Dihydropterin 100%
• Conformational Transition 100%
• ATP 66%
• NMR Signal 66%
• Folate 33%
• Kd 33%
• Cofactor 33%
• catalytic cycle 33%
• solution structure 33%
• Protein Dynamics 33%