Measurement and characterization of binding interactions between proteins and low-molecular weight (LMW) ligands are a focus of academic research and drug discovery. Isothermal titration calorimetry (ITC) directly measures heat released or absorbed in a binding event, providing means for studying protein-small molecule interactions in solution without the need for labeling or immobilization. Importantly, ITC is often utilized to characterize differences in entropic and enthalpic contributions to binding of novel ligands.
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