Quantitative analysis of ligand-macromolecule interactions using differential dynamic quenching of the ligand fluorescence to monitor the binding

Keyphrases

• Binding Site 20%
• Binding Studies 20%
• Biological Systems 20%
• Bound States 20%
• Collisional Dynamics 20%
• Collisional Quenching 20%
• Complex Formation 20%
• Cooperative Ligands 20%
• Differential Dynamics 100%
• Dynamic Quenching 100%
• Escherichia Coli 20%
• External Dynamics 20%
• Fluorescence Change 40%
• Fluorescence Property 20%
• Fluorescence Titration 20%
• Fluorescent Compounds 20%
• Fluorescent Ligand 20%
• Fluorophore 20%
• Free State 20%
• Hexamer 20%
• Interacting Species 20%
• Intrinsic Fluorescence 20%
• Kinetic Parameters 20%
• Kinetic Study 20%
• Macromolecule Interactions 100%
• Macromolecules 100%
• Monitoring Change 20%
• Multiple Ligands 20%
• Nonoperative 20%
• Nucleotide Cofactor 20%
• Quencher 40%
• Quenching Process 20%
• Replicative Helicase 20%
• Spectroscopic Properties 20%
• Thermodynamics 40%
• Unbound States 20%

Biochemistry, Genetics and Molecular Biology

• Adenosine Diphosphate 12%
• Binding Site 12%
• Complex Formation 12%
• DnaB Helicase 12%
• Escherichia coli 12%
• Helicase 12%
• Kinetic Parameter 12%
• Ligand Binding 12%
• Macromolecule 100%
• Quantitative Technique 100%
• Solution and Solubility 12%

Chemistry

• Ammonium Dihydrogen Phosphate 12%
• Binding Site 12%
• Bound State 12%
• Cofactor 12%
• Collisional 25%
• formation 25%
• Kinetic Study 12%
• Macromolecule 100%
• Pharmacokinetics 12%