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Related Concept Videos

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

The equilibrium binding constant (Kb) quantifies the strength of a protein-ligand interaction. Kb can be calculated as follows when the reaction is at equilibrium:
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...
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...
Thermal Sigmatropic Reactions: Overview01:16

Thermal Sigmatropic Reactions: Overview

Sigmatropic rearrangements are a class of pericyclic reactions in which a σ bond migrates from one part of a π system to another. These are intramolecular rearrangements where the total number of σ and π bonds remain unchanged.
Sigmatropic shifts are classified based on an order term [i, j ], where i and j indicate the number of atoms across which each end of the σ bond migrates. Below are examples of a [3,3] sigmatropic shift in 1,5-hexadiene, referred to as...

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Related Experiment Video

Updated: Jun 24, 2026

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
08:45

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

Isothermal titration calorimetry: general formalism using binding polynomials.

Ernesto Freire1, Arne Schön, Adrian Velazquez-Campoy

  • 1Department of Biology, Johns Hopkins University, Baltimore, Maryland, USA.

Methods in Enzymology
|March 18, 2009
PubMed
Summary
This summary is machine-generated.

The binding polynomial formalism offers a unified, model-free approach to analyze complex ligand binding data from isothermal titration calorimetry (ITC). This method reveals binding cooperativity and provides accurate association constants and enthalpy values.

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Published on: August 23, 2022

Area of Science:

  • Biochemistry
  • Biophysics
  • Chemical Thermodynamics

Background:

  • Analyzing ligand binding in biological systems, particularly with multiple binding sites, is often complex.
  • Traditional isothermal titration calorimetry (ITC) data analysis requires specific binding models, which can be ambiguous or difficult to determine.
  • Distinguishing between different binding mechanisms using only binding isotherms can be challenging due to model degeneracy.

Purpose of the Study:

  • To introduce the binding polynomial formalism as a powerful, unified framework for analyzing experimental biological ligand binding data.
  • To demonstrate the advantages of a model-free methodology for interpreting isothermal titration calorimetry (ITC) data, especially for systems with multiple binding sites.
  • To provide a method for extracting essential information about binding cooperativity and thermodynamic parameters without prior model assumptions.

Main Methods:

  • Application of the general binding polynomial formalism to analyze experimental data.
  • Utilizing a model-free methodology to interpret isothermal titration calorimetry (ITC) data.
  • Theoretical and experimental examples illustrating the formalism's use in ligand binding studies.

Main Results:

  • The binding polynomial formalism enables model-free analysis of ligand binding, simplifying complex ITC data interpretation.
  • The approach successfully identifies the presence and nature (positive or negative) of binding cooperativity and quantifies cooperative energy.
  • Derived binding association constants and enthalpy values remain valid and can be readily translated into model-specific parameters once the correct binding model is established.

Conclusions:

  • The binding polynomial formalism provides a robust and versatile tool for the unified analysis of diverse ligand binding phenomena.
  • This method overcomes limitations of traditional model-dependent approaches in ITC, offering deeper insights into binding mechanisms and cooperativity.
  • The formalism facilitates accurate determination of thermodynamic parameters, enhancing the understanding of molecular interactions in biological systems.