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Related Concept Videos

Calorimetry01:19

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...
Constant Pressure Calorimetry03:02

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 Calorimetry02:41

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 Strategies01:08

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...
EDTA: Indirect and Alkalimetric Titration01:23

EDTA: Indirect and Alkalimetric Titration

Unlike direct titration, back-titration, and displacement titration, indirect titration is an EDTA titration method for quantifying anions. In the indirect titration method, anions are precipitated as their insoluble salts with excess metal ions. The filtrate containing the excess metal ions is directly titrated with standard EDTA until the endpoint is achieved. Another approach involves extracting the metal ion and back-titrating with standard EDTA to obtain the endpoint. In this way, the...
Redox Titration: Iodimetry and Iodometry01:23

Redox Titration: Iodimetry and Iodometry

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...

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Related Experiment Video

Updated: Jul 7, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
08:37

Measuring Enzymatic Stability by Isothermal Titration Calorimetry

Published on: March 26, 2019

Isothermal titration calorimetry.

Adrián Velázquez-Campoy1, Hiroyasu Ohtaka, Azin Nezami

  • 1Johns Hopkins University, Baltimore, Maryland, USA.

Current Protocols in Cell Biology
|January 30, 2008
PubMed
Summary
This summary is machine-generated.

Isothermal titration calorimetry (ITC) is a key method for analyzing biological binding. This study presents diverse ITC protocols for various binding affinities and special cases.

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Last Updated: Jul 7, 2026

Measuring Enzymatic Stability by Isothermal Titration Calorimetry
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Published on: March 26, 2019

Hot Biological Catalysis: Isothermal Titration Calorimetry to Characterize Enzymatic Reactions
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Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
08:45

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Isothermal titration calorimetry (ITC) is widely adopted for characterizing binding energetics in biological systems.
  • ITC enables the study of diverse interactions like protein-ligand, protein-protein, and DNA-protein binding.

Purpose of the Study:

  • To present a comprehensive set of isothermal titration calorimetry (ITC) protocols.
  • To cover basic to advanced applications for determining binding affinities.
  • To address special cases and additional thermodynamic information.

Main Methods:

  • Detailed protocols for isothermal titration calorimetry (ITC) are provided.
  • Methods range from basic characterization of moderate affinity binding to advanced techniques for high or low affinity interactions.
  • Specialized protocols for homodimeric and unstable proteins are included.

Main Results:

  • The presented protocols facilitate the accurate determination of binding energetics across a wide affinity spectrum.
  • The study details methods for characterizing various biological binding events, including protein-ligand and protein-protein interactions.
  • Additional insights into heat capacity and coupled protonation/deprotonation processes are accessible via ITC.

Conclusions:

  • This unit offers a valuable resource of ITC protocols for researchers studying molecular interactions.
  • The presented methods enhance the capability to precisely quantify binding thermodynamics for diverse biological systems.
  • ITC is demonstrated as a versatile tool for comprehensive analysis of binding events and associated thermodynamic parameters.