Allostery and binding cooperativity of the catalytic subunit of protein kinase a by NMR spectroscopy and molecular dynamics simulations

Keyphrases

• Protein Kinase 100%
• NMR Spectroscopy 100%
• Molecular Dynamics Simulation 100%
• Conformational Dynamics 100%
• Allostery 100%
• Allosteric Activation 100%
• Catalytic Subunit 100%
• Binding Cooperativity 100%
• Study Support 50%
• Single Molecule 50%
• Bound States 50%
• Conformational Entropy 50%
• Ligand Binding 50%
• Catalytic Cycle 50%
• Substrate Binding 50%
• Internal Dynamics 50%
• Allosteric Enzyme 50%
• Free State 50%
• Nucleotide Binding 50%
• Inhibitor Binding 50%
• Enzymatic Function 50%
• Free Energy Landscape 50%
• Enthalpic Interaction 50%
• Quenched State 50%
• Enzyme Conformational Dynamics 50%
• CAMP-dependent Protein Kinase 50%
• Dynamic Signaling 50%

Biochemistry, Genetics and Molecular Biology

• Dynamics 100%
• Nuclear Magnetic Resonance Spectroscopy 100%
• Allosteric Regulation 100%
• Cooperation 100%
• Enzyme Active Site 100%
• Protein Kinases 100%
• Protein Kinase A 100%
• Enzyme 50%
• Ligand Binding 25%
• Energy Landscape 25%
• Conformational Entropy 25%
• Allosteric Enzyme 25%
• Enzyme Activity 25%
• Cyclic Adenosine Monophosphate 25%