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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.
View history; General ... such as differential scanning calorimetry or isothermal titration calorimetry due to various effects other ... example figure, the reaction ...
A calorimeter is a device used for calorimetry, or the process of measuring the heat of chemical reactions or physical changes as well as heat capacity. Differential scanning calorimeters, isothermal micro calorimeters, titration calorimeters and accelerated rate calorimeters are among the most common types. A simple calorimeter just consists ...
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 ...
Calorimetry is the science of measuring the heat of chemical reactions or physical changes. Calorimetry is performed with a calorimeter.. Isothermal microcalorimetry (IMC) is a laboratory method for real-time, continuous measurement of the heat flow rate (μJ/s = μW) and cumulative amount of heat (J) consumed or produced at essentially constant temperature by a specimen placed in an IMC ...
In biochemistry, formation constants of adducts may be obtained from Isothermal titration calorimetry (ITC) measurements. This technique yields both the stability constant and the standard enthalpy change for the equilibrium. [45] It is mostly limited, by availability of software, to complexes of 1:1 stoichiometry.
The thermodynamics of the host- guest interaction can be assessed by NMR spectroscopy, UV/visible spectroscopy, and isothermal titration calorimetry. [9] Quantitative analysis of binding constant values provides useful thermodynamic information. [citation needed]