Quantitative Relationships of Site to Site Interaction in Escherichia coli D-3-Phosphoglycerate Dehydrogenase Revealed by Asymmetric Hybrid Tetramers

Keyphrases

• Escherichia Coli 100%
• Active Sites 100%
• Glyceraldehyde-3-phosphate Dehydrogenase 100%
• Asymmetric Hybridization 100%
• Quantitative Relationship 100%
• Positive Cooperativity 50%
• Effector Molecules 50%
• Effector Binding 50%
• Domain Interface 50%
• Binding Site 25%
• Co-expression 25%
• Conformational Change 25%
• Ligand Binding 25%
• Inhibition Rate 25%
• Regulatory Domain 25%
• Two-site 25%
• Inhibition Profiles 25%
• Allostery 25%
• Quantitative Effects 25%
• Site Activity 25%
• Active Binding Site 25%
• Number of Active Sites 25%
• Maximum Inhibition 25%
• Nucleotide-binding Domain 25%
• Simple Rules 25%

Biochemistry, Genetics and Molecular Biology

• Active Site 100%
• Escherichia coli 100%
• Phosphoglycerate Dehydrogenase 100%
• Cooperation 40%
• Binding Site 20%
• Enzyme 20%
• Binding Domain 20%
• Conformational Change 20%
• Ligand Binding 20%
• Allosteric Regulation 20%