Thermal Shift Assays are an ideal way to identify ligands that are able to specifically bind to a target protein of interest by measuring the thermal stability of a protein, which is intrinsically linked to its environment. In conditions that increase the stability of a target protein, such as optimal pH, optimal buffer conditions, or the specific binding of a ligand to a protein, the protein has increased thermal stability. We are able to exploit this phenomenon through the use of fluorescent dyes which bind to exposed hydrophobic residues on proteins to monitor protein stability in real time.
At o2h we can offer the use of thermal shift assays to detect real time changes in protein stability for the following purposes:
- Screening small molecules to detect ligand-protein interactions
- Identify optimal conditions (pH/buffer composition) for protein stability
- Identify key residues for ligand-binding in a protein of interest by utilizing our expertise in site-directed mutagenesis
- Complements other biophysical methods like Fluorescence Polarization (FP) and Surface Plasmon Resonance (SPR)
To know more about our biology services offering or to request our brochure, please reach out to us at discovery@o2h.com.
