The αC-β4 loop controls the allosteric cooperativity between nucleotide and substrate in the catalytic subunit of protein kinase A

Keyphrases

• Excited States 100%
• Protein Kinase 100%
• Catalytic Subunit 100%
• Allosteric Cooperativity 100%
• Loop Control 100%
• Substrate Recognition 33%
• Structural Response 33%
• Spine 33%
• Drug Sensitivity 33%
• Conformational Transition 33%
• Nuclear Magnetic Resonance 33%
• Synergistic Interaction 33%
• Catalytic Efficiency 33%
• Free Energy 33%
• Two-lobe 33%
• Substrate Binding 33%
• Loop Conformation 33%
• Inactive State 33%
• Conformational Ensemble 33%
• Binding Partners 33%
• Active State 33%
• Synergistic Action 33%
• Allosteric Binding 33%
• Swinging 33%
• First Excited State 33%
• Apoenzyme 33%
• ATP Binding 33%
• Regulatory Subunit 33%
• Binding Cooperativity 33%
• Free Energy Landscape 33%
• Hydrophobic Packing 33%
• Restrained Molecular Dynamics Simulations 33%
• C-helix 33%
• Markov State Model 33%
• F100 33%
• Landscape Transitions 33%

Biochemistry, Genetics and Molecular Biology

• Cooperation 100%
• Enzyme Active Site 100%
• Protein Kinase A 100%
• Adenosine Triphosphate 66%
• Magnetism 33%
• Conformation 33%
• Conformational Change 33%
• Conformational Ensembles 33%
• Energy Landscape 33%
• Catalytic Efficiency 33%
• Drug Sensitivity 33%
• Cyclic Adenosine Monophosphate 33%
• Computer Simulation 33%