Isothermal titration calorimetry (ITC) is a biophysical technique that allows a thermodynamic
characterization of an interactive system. It is a free in solution technique that requires no …

Calorimetry is a classical biophysical method that by definition measures heat. In isothermal
titration calorimetry (ITC), the heat is the result of titrating interacting components together …

Isothermal titration calorimetry (ITC) is a fast, accurate and label‐free method for measuring
the thermodynamics and binding affinities of molecular associations in solution. Because the …

The analysis of protein-protein interactions has attracted the attention of many researchers
from both a fundamental point of view and a practical point of view. From a fundamental …

Isothermal titration calorimetry (ITC) is one of the main techniques to determine specific
interactions between molecules dissolved in aqueous solution. This technique is commonly …

Isothermal titration calorimetry is an ideal technique for measuring biological binding
interactions. It does not rely on the presence of chromophores or fluorophores, nor does it …

This protocol can be applied to analyze the direct interaction between a soluble protein and
a target ligand molecule using Isothermal Titration Calorimetry (ITC, Malvern). ITC allows the …

Isothermal titration calorimetry (ITC) is perhaps the most rigorous commercially available
method for characterizing protein‐ligand interactions. In this method, interactions are …

Isothermal titration calorimetry (ITC) is a useful tool for understanding the complete
thermodynamic picture of a binding reaction. In biological sciences, macromolecular …

The binding of two biomolecules viewed from the atomic level is highly complex. It involves
the formation or removal of many individual non-covalent bonds both between the …