A network of conserved interactions regulates the allosteric signal in a glutamine amidotransferase

Keyphrases

• β-glycerophosphate 100%
• Imidazole 100%
• Glutamine Amidotransferase 100%
• Conserved Interactions 100%
• Steered Molecular Dynamics Simulation 66%
• Active Sites 66%
• Principal Coordinate Analysis (PCoA) 66%
• Correlation Analysis 66%
• Ribonucleotides 66%
• Allosteric Regulation 66%
• Coupled Motion 66%
• Allosteric Transition 66%
• Equilibration 33%
• Binding Site 33%
• Correlated Motion 33%
• Atomic Resolution 33%
• Protein Motion 33%
• Conserved Residues 33%
• Equilibrium Molecular Dynamics Simulation 33%
• Network Routing 33%
• Substrate Binding Site 33%
• Kinetic Assay 33%
• Evolutionary Analysis 33%
• Undocking 33%
• Interaction Network 33%
• Glutaminase 1 (GLS1) 33%
• Carboxamide 33%
• 5-Aminoimidazoles 33%
• Effector Binding 33%

Biochemistry, Genetics and Molecular Biology

• Motion 100%
• Glutamine Amidotransferase 100%
• Dynamics 60%
• Synthase 60%
• Glycerol 60%
• Active Site 40%
• Binding Site 40%
• Ribonucleotide 40%
• Allosteric Regulation 40%
• Wild Type 20%
• Principal Component Analysis 20%
• Glutaminase 20%