Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

15.5K
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:
15.5K
The Equilibrium Binding Constant and Binding Strength02:18

The Equilibrium Binding Constant and Binding Strength

10.7K
10.7K
Ligand Binding Sites02:40

Ligand Binding Sites

15.6K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
15.6K
Complexation Equilibria: Overview01:23

Complexation Equilibria: Overview

1.6K
Complexation reactions take place when dative or coordinate covalent bonds form between metal ions and ligands. The compounds formed in these reactions are called coordination compounds. The number of bonds formed between the metal ion and the ligands is called its coordination number. Generally, most metal ions in an aqueous solution are solvated by water molecules and thus exist as aqua complexes.
The equilibrium constant of the complexation reaction is represented as the formation constant...
1.6K
Conserved Binding Sites01:49

Conserved Binding Sites

5.3K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
5.3K
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

5.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
5.8K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The Concise Guide to PHARMACOLOGY 2025/26: Ion channels.

British journal of pharmacology·2025
Same author

BK channel activity in skin fibroblasts from patients with neurological disorder.

Channels (Austin, Tex.)·2025
Same author

The Concise Guide to PHARMACOLOGY 2023/24: Ion channels.

British journal of pharmacology·2023
Same author

Implications of a temperature-dependent heat capacity for temperature-gated ion channels.

Proceedings of the National Academy of Sciences of the United States of America·2023
Same author

Calcium dependence of both lobes of calmodulin is involved in binding to a cytoplasmic domain of SK channels.

eLife·2022
Same author

The surprising difficulty of "simple" equilibrium binding measurements on ligand-gated ion channels.

The Journal of general physiology·2022

Related Experiment Video

Updated: Mar 9, 2026

Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
12:38

Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction

Published on: February 15, 2018

20.9K

Structural identifiability of equilibrium ligand-binding parameters.

Thomas R Middendorf1,2, Richard W Aldrich3,2

  • 1Center for Learning and Memory, University of Texas at Austin, Austin, TX 78712.

The Journal of General Physiology
|December 21, 2016
PubMed
Summary

This study introduces a method to determine if protein-ligand binding parameters are uniquely identifiable. It reveals a universal mathematical structure for binding relations, ensuring parameter identifiability for robust experimental design.

More Related Videos

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

63.0K
Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
08:45

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

54.3K

Related Experiment Videos

Last Updated: Mar 9, 2026

Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction
12:38

Titration ELISA as a Method to Determine the Dissociation Constant of Receptor Ligand Interaction

Published on: February 15, 2018

20.9K
Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
13:26

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

63.0K
Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
08:45

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity

Published on: September 7, 2011

54.3K

Area of Science:

  • Biophysics
  • Biochemistry
  • Systems Biology

Background:

  • Protein-ligand interactions are crucial for biological processes.
  • Key molecular properties like binding affinities and cooperativity are not directly measurable.
  • These properties are typically estimated using models fitted to binding data.

Purpose of the Study:

  • To develop a general method for assessing the identifiability of protein-ligand binding parameters.
  • To provide insights into the causes of non-unique parameter estimates.
  • To guide the design and analysis of protein-ligand binding experiments.

Main Methods:

  • Analysis of equilibrium total binding relations.
  • Reduction of binding relations to conserved mathematical forms.
  • Application of matrix algebraic methods to prove structural identifiability (SI).

Main Results:

  • A conserved mathematical form for binding relations in bimolecular association models was identified.
  • A related conserved form was found for models with binding and conformational equilibria.
  • Universal parameterization of binding relations was shown to be structurally identifiable for various protein models.

Conclusions:

  • The study establishes a universal mathematical framework for protein-ligand binding.
  • The derived parameterization ensures structural identifiability of binding properties.
  • This work provides a foundation for understanding practical identifiability in real-world experimental data.