Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

The Equilibrium Binding Constant and Binding Strength

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 Strength

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:

Protein-Drug Binding: Determination Methods

Protein-Drug Binding: Determination Methods

Determining protein-drug binding can be achieved through indirect and direct methods, each providing valuable insights into the interaction between proteins and drugs.
Indirect methods involve isolating the bound drug from its free form in biological samples such as blood, serum, or plasma. These techniques aim to measure the percentage of drugs bound to proteins. Equilibrium dialysis is a commonly used method where the free drug concentration at equilibrium is measured by separating the bound...

Cooperative Binding of Transcription Regulators

Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome. Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...

Conserved Binding Sites

Conserved Binding Sites

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 analyses the...

Conserved Binding Sites

Conserved Binding Sites

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 analyses the...

You might also read

Related Articles

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

Sort by

Same author

Deep-learning-based de novo discovery and design of therapeutics that reverse disease-associated transcriptional phenotypes.

Cell·2026

Same author

The Concise Guide to PHARMACOLOGY 2025/26: G protein-coupled receptors.

British journal of pharmacology·2025

Same author

Pirin does not bind to p65 or regulate NFκB-dependent gene expression but does modulate cellular quercetin levels.

Molecular pharmacology·2025

Same author

Reversion of a RND transporter pseudogene reveals latent stress resistance potential in Brucella ovis.

PLoS genetics·2025

Same author

Reversion of a RND transporter pseudogene uncovers latent stress resistance in <i>Brucella ovis</i>.

bioRxiv : the preprint server for biology·2025

Same author

Analyzing lognormal data: A nonmathematical practical guide.

Pharmacological reviews·2025

Same journal

Simultaneous Ca<sup>2+</sup> Imaging and Optogenetic Stimulation of Cortical Astrocytes in Adult Murine Brain Slices.

Current protocols in neuroscience·2020

Same journal

Automated Two-Chamber Operon ID/ED Task for Mice.

Current protocols in neuroscience·2020

Same journal

A Guide to Fluorescence Lifetime Microscopy and Förster's Resonance Energy Transfer in Neuroscience.

Current protocols in neuroscience·2020

Same journal

Development, Screening, and Validation of Camelid-Derived Nanobodies for Neuroscience Research.

Current protocols in neuroscience·2020

Same journal

Recombinant Antibodies in Basic Neuroscience Research.

Current protocols in neuroscience·2020

Same journal

Automated Quantification of Mitochondrial Fragmentation in an In Vitro Parkinson's Disease Model.

Current protocols in neuroscience·2020

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 12, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

Analyzing binding data.

Harvey J Motulsky¹, Richard R Neubig

¹GraphPad Software, La Jolla, California, USA.

Current Protocols in Neuroscience

|June 26, 2010

Summary

This summary is machine-generated.

This study details how to measure radioligand binding kinetics. Understanding binding site characteristics like affinity and accessibility is crucial for drug development.

More Related Videos

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Related Experiment Videos

Last Updated: Jun 12, 2026

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Area of Science:

Pharmacology
Biochemistry
Molecular Biology

Background:

Radioligand binding assays are fundamental in pharmacology.
Quantifying binding parameters informs drug discovery and development.

Purpose of the Study:

To provide a comprehensive guide on designing and analyzing radioligand binding experiments.
To elucidate the number, affinity, and accessibility of drug targets.

Main Methods:

Experimental design for radioligand binding studies.
Kinetic and equilibrium binding data analysis.
Scatchard and other relevant plotting methods.

Main Results:

Determination of receptor density (Bmax).
Calculation of dissociation constant (Kd) and association/dissociation rates (kon/koff).
Assessment of drug-target interactions and drug efficacy.

Conclusions:

Accurate measurement of radioligand binding is essential for characterizing drug-target interactions.
This unit provides a framework for robust experimental design and data interpretation in drug research.