Can XRD or any other biophysical methods other than ITC be used to study the interaction between a protein and a small ligand molecule ?
In principle, any technique that can distinguish the protein in its free state from its complexed state could allow you to quantify the binding equilibrium constant (Kb), and then the binding free energy. Then, you can obtain Kb at different temperatures and then estimate the binding enthalpy through the van't Hoff 's method. Spectroscopic methods such as UV-Vis Differential Absorption or Fluorescence could be useful in this respect.
You can try to use XRD if the interaction leads to at an arrangement of protein and ligand.
The ITC and DSC are the best technique for interaction study between a protein and a small ligand for get some important biothermodynamic and energetic parameters. These parameter can distinguish and comparing stability of conjugate product to other. However some of easy and enough accurate spectroscopic methods such as CD, UV, Fluorescence and .. could be useful for achieve the structural changes in interaction study.
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