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Related Concept Videos

Calorimetry01:19

Calorimetry

3.5K
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...
3.5K
Constant Pressure Calorimetry03:02

Constant Pressure Calorimetry

93.7K
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...
93.7K
Constant Volume Calorimetry02:41

Constant Volume Calorimetry

29.2K
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...
29.2K
Titrimetric Methods: Types and Commonly Used Strategies01:08

Titrimetric Methods: Types and Commonly Used Strategies

1.3K
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...
1.3K
Redox Titration: Iodimetry and Iodometry01:23

Redox Titration: Iodimetry and Iodometry

3.8K
Iodometry and iodimetry are analytical methods used to determine the concentration of oxidizing or reducing agents using iodine. In iodometric titrations, the oxidizing analyte solution is usually acidified and treated with an excess of iodide ions, which generates an equivalent amount of iodine in equilibrium with triiodide. The released iodine is subsequently titrated directly against a standardized reducing agent. As the dilute iodine color becomes pale yellow, a few drops of freshly...
3.8K
Temperature and Thermal Equilibrium01:11

Temperature and Thermal Equilibrium

8.0K
Heat and temperature are essential concepts for everyone every day. The study of heat and temperature is part of an area of physics known as thermodynamics. It is not always easy to distinguish heat and temperature.
The concept of temperature has evolved from the common concepts of hot and cold. The scientific definition of temperature explains more than just our sense of hot and cold. Temperature is operationally defined as the quantity measured with a thermometer. Furthermore, temperature is...
8.0K

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Related Experiment Video

Updated: Nov 8, 2025

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
08:37

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

13.9K

Isothermal Titration Calorimetry.

Christopher M Johnson1

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK. cmj@mrc-lmb.cam.ac.uk.

Methods in Molecular Biology (Clifton, N.J.)
|April 20, 2021
PubMed
Summary
This summary is machine-generated.

Isothermal titration calorimetry (ITC) quantifies the thermodynamics of molecular interactions by measuring heat changes. This biophysical technique aids in understanding protein-protein interactions and guiding rational ligand design.

Keywords:
Binding affinityBinding kineticsDissociation constantEnthalpyEntropyFree energyHeat capacityITCIsothermal titration calorimetryStoichiometryThermodynamics

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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

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Last Updated: Nov 8, 2025

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
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Measuring Enzymatic Stability by Isothermal Titration Calorimetry

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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions

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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

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Area of Science:

  • Biophysics
  • Biochemistry
  • Molecular Biology

Background:

  • Calorimetry is a fundamental biophysical method for measuring heat.
  • Isothermal titration calorimetry (ITC) directly quantifies the thermodynamics of molecular interactions.
  • Understanding binding thermodynamics is crucial for rational drug design and molecular interaction studies.

Purpose of the Study:

  • To highlight the utility of isothermal titration calorimetry (ITC) in biophysical research.
  • To explain how ITC enables direct determination of binding thermodynamics.
  • To discuss the application of ITC in rational ligand design and protein-protein interaction analysis.

Main Methods:

  • Isothermal titration calorimetry (ITC) measures heat changes resulting from the titration of interacting components.
  • Analysis of heat changes allows for direct determination of enthalpy change (ΔH).
  • ITC data provides thermodynamic parameters for molecular binding events.

Main Results:

  • ITC directly quantifies the enthalpy change (ΔH) of molecular interactions.
  • The technique is valuable for studying protein-protein interactions.
  • ITC facilitates thermodynamics-guided rational design of ligands.

Conclusions:

  • Isothermal titration calorimetry (ITC) is an established technique for quantifying molecular interaction thermodynamics.
  • Despite limitations related to solvent participation, ITC is a powerful tool in biophysical research.
  • Careful application of ITC offers insights into binding processes and complex molecular events.