Probing the regulatory domain interface of D-3-phosphoglycerate dehydrogenase with engineered tryptophan residues

Keyphrases

• Regulatory Domain 100%
• Glyceraldehyde-3-phosphate Dehydrogenase 100%
• Tryptophan Residues 100%
• Domain Interface 100%
• Conformational Change 66%
• Fluorescence Quenching 66%
• Binding Site 33%
• Escherichia Coli 33%
• Helix 33%
• Active Sites 33%
• Hydrogen Bonds (H-bonds) 33%
• Enzymatic Activity 33%
• Hydrogen Bond Network 33%
• Two-component Domains 33%
• Binding Studies 33%
• Effector Binding 33%
• Allosteric Mechanism 33%
• Enzymatic Inhibition 33%
• Non-covalent Association 33%
• Rigid Domain 33%
• Tryptophan Quenching 33%
• Regulatory Interface 33%

Biochemistry, Genetics and Molecular Biology

• Phosphoglycerate Dehydrogenase 100%
• Tryptophan 100%
• Serine 100%
• Enzyme 18%
• Conformational Change 18%
• Quenching (Fluorescence) 18%
• Binding Site 9%
• Active Site 9%
• Escherichia coli 9%
• Hydrogen Bond 9%
• Enzyme Activity 9%
• Binding Study 9%