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Constant Pressure Calorimetry

Constant Pressure Calorimetry

Calorimetry is a technique used to measure the amount of heat involved in a chemical or physical process or to measure the heat transferred to or from a substance. The heat is exchanged with a calibrated and insulated device called the calorimeter. Calorimetry experiments are based on the assumption that there is no heat exchange between the insulated calorimeter and the external environment. The well-insulated calorimeters prevent the transfer of heat between the calorimeter and its external...

Constant Volume Calorimetry

Constant Volume Calorimetry

Calorimeters are useful to determine the heat released or absorbed by a chemical reaction. Coffee cup calorimeters are designed to operate at constant (atmospheric) pressure and are convenient to measure heat flow (or enthalpy change) accompanying processes that occur in solution at constant pressure. A different type of calorimeter that operates at constant volume, colloquially known as a bomb calorimeter, is used to measure the energy produced by reactions that yield large amounts of heat and...

Titrimetric Methods: Types and Commonly Used Strategies

Titrimetric Methods: Types and Commonly Used Strategies

In chemistry, titrimetric methods are broadly classified into three types: volumetric, gravimetric, and coulometric. Volumetric titrations involve measuring the volume of a titrant of known concentration that is required to react completely with an analyte. In gravimetric titrations, the standard solution reacts with the analyte to form an insoluble precipitate, which is filtered, dried, and weighed. In coulometric titrations, current is applied to an electrochemical reaction until the reaction...

Controlled-Current Coulometry: Coulometric Titration

Controlled-Current Coulometry: Coulometric Titration

Coulometric titrations are a form of titrimetric analysis where the reagent is generated electrically, and its amount is evaluated based on current and generating time. The electron serves as the standard reagent. The procedure is similar to conventional titrations, such as endpoint detection.
The fundamental requirements for coulometric titrations are (1) 100% efficiency in the reagent-generating electrode reaction and (2) a stoichiometric and preferably rapid reaction between the generated...

Calorimetry

Calorimetry

When objects at different temperatures are placed in contact with each other but isolated from everything else, they attain thermal equilibrium. A container that prevents heat transfer in or out is called a calorimeter, and the use of a calorimeter to make measurements is called calorimetry. Generally, these measurements involve heat or specific heat capacity. The term "calorimetry problem" is used for any problem where the specified objects are thermally isolated from their surroundings. An...

Complexometric Titration: Overview

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Complexometric titration involves the formation of a complex by reacting a metal ion with one or more ligands. A visual indicator often detects the end point of a complexometric titration. It is added to the metal solution before the titration, forming a stable metal–indicator complex and imparting color to the solution. As the titration approaches the equivalence point, the excess of the added ligand displaces the indicator from the metal–indicator complex, releasing the free indicator. The...

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Updated: Jul 5, 2026

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

Titration microcalorimetry.

¹SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania, USA.

Current Protocols in Protein Science

|April 23, 2008

Summary

Isothermal titration calorimetry (ITC) rigorously characterizes protein-ligand interactions by detecting binding enthalpy changes in native proteins. This method provides thermodynamic insights into molecular binding mechanisms.

Area of Science:

Biochemistry
Biophysics
Molecular Biology

Background:

Protein-ligand interactions are fundamental to biological processes.
Accurate characterization of these interactions is crucial for understanding molecular mechanisms.
Existing methods may require protein modification or surface attachment, potentially altering behavior.

Purpose of the Study:

To highlight Isothermal Titration Calorimetry (ITC) as a rigorous method for studying protein-ligand interactions.
To emphasize the advantages of ITC for analyzing native, unmodified proteins in solution.
To showcase the versatility of ITC in addressing qualitative and quantitative binding questions.

Main Methods:

Isothermal Titration Calorimetry (ITC) measures the heat changes associated with molecular binding events.

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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

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Last Updated: Jul 5, 2026

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

Published on: April 4, 2014

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

The technique analyzes interactions of native proteins in their solution state.

Proper control experiments are essential for accurate thermodynamic data acquisition.

Main Results:

ITC directly detects the binding enthalpy change, providing a direct measure of interaction.
The method is applicable to proteins that are sensitive to chemical modification or surface immobilization.
ITC can confirm the occurrence of binding and quantify the concentration of active protein.

Conclusions:

Isothermal Titration Calorimetry is a powerful and versatile tool for characterizing protein-ligand interactions.
Its ability to study native proteins makes it invaluable for biological research.
ITC offers rich thermodynamic information essential for elucidating molecular binding mechanisms.