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In chemical thermodynamics, isothermal titration calorimetry (ITC) is a physical technique used to determine the thermodynamic parameters of interactions in solution. [ 1 ] [ 2 ] It is most often used to study the binding of small molecules (such as medicinal compounds) to larger macromolecules ( proteins , DNA etc.) in a label-free environment.
Isothermal titration calorimeter An isothermal titration calorimeter uses the heat produced or consumed by the reaction to determine the equivalence point. This is important in biochemical titrations, such as the determination of how substrates bind to enzymes .
In an isothermal titration calorimeter, the heat of reaction is used to follow a titration experiment. This permits determination of the midpoint ( stoichiometry ) (N) of a reaction as well as its enthalpy (delta H), entropy (delta S) and of primary concern the binding affinity (Ka)
Calorimetry requires that a reference material that changes temperature have known definite thermal constitutive properties. The classical rule, recognized by Clausius and Kelvin, is that the pressure exerted by the calorimetric material is fully and rapidly determined solely by its temperature and volume; this rule is for changes that do not involve phase change, such as melting of ice.
Isothermal titration calorimetry (ITC), is considered as the most quantitative technique available for measuring the thermodynamic properties of protein–protein interactions and is becoming a necessary tool for protein–protein complex structural studies. This technique relies upon the accurate measurement of heat changes that follow the ...
The aggregation number of micelles can be determined by isothermal titration calorimetry when the aggregation number is not too high. [2] [3] Another classical experiment to determine the mean aggregation number would involve the use of a luminescent probe, a quencher and a known concentration of surfactant. If the concentration of the quencher ...
which is equivalent to the Scatchard equation. ... Many modern methods for measuring binding such as surface plasmon resonance and isothermal titration calorimetry ...
The others are Spectrophotometric, Fluorescence (luminescence) measurements and NMR chemical shift measurements; [8] [17] simultaneous measurement of K and ΔH for 1:1 adducts in biological systems is routinely carried out using Isothermal Titration Calorimetry. The experimental data will comprise a set of data points.