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

Ligand Binding Sites

Ligand Binding Sites

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...

Ligand Binding Sites

Ligand Binding Sites

Protein-Drug Binding: Mechanism and Kinetics

Protein-Drug Binding: Mechanism and Kinetics

Protein-drug binding refers to the interaction between drugs and proteins within the body. This binding process can occur intracellularly, involving drug interactions with enzymes or receptors within cells, or extracellularly, involving plasma proteins in the blood.
Various forces drive these interactions, including hydrogen bonds, hydrophobic interactions, ionic bonds, electrostatic interactions, and van der Waals forces. These bonds enable drugs to bind to specific sites on proteins,...

Quantitative Aspects of Drug-Receptor Interaction

Quantitative Aspects of Drug-Receptor Interaction

The receptor occupancy theory connects a drug's response to the number of occupied receptors. With higher drug concentrations, more receptors are occupied, leading to increased responses. The formation of drug-receptor complexes involves association and dissociation rates, which reach equilibrium when the forward and backward reactions are equal. The equilibrium association constant (Ka) and its inverse, the equilibrium dissociation constant (Kd), indicate drug affinity. Higher Ka and lower...

You might also read

Related Articles

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

Sort by

Same author

Fluctuation-driven mass-selective transport in dynamic nanopores.

Nature communications·2026

Same author

TDTAC: a generalized time-dependent torsion angle correlation framework for resolving directional coordination in large biomolecular assemblies.

Frontiers in molecular biosciences·2026

Same author

Cationic imidazolium macrocycles enable array-based, site-selective optical detection of peptide phosphorylation.

Organic & biomolecular chemistry·2026

Same author

Revealing Imatinib-Kinase Specificity via Analyzing Changes in Protein Dynamics and Computing Molecular Binding Affinity.

The journal of physical chemistry. B·2026

Same author

CACNA1C as a Prognostic Biomarker and Therapeutic Target in High-Grade Serous Ovarian Cancer: Clinical Validation and Molecular Dynamics of Nifedipine Blockade.

bioRxiv : the preprint server for biology·2026

Same author

Super-Arrhenius dynamic slowdown revealed by slow variable modulation in the fragile supercooled liquid.

The Journal of chemical physics·2026

Search research articles

Related Experiment Video

Updated: Mar 12, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

Understanding ligand-receptor non-covalent binding kinetics using molecular modeling.

Zhiye Tang¹, Christopher C Roberts¹, Chia-En A Chang²

¹Department of Chemistry, University of California, Riverside, CA 92521.

Frontiers in Bioscience (Landmark Edition)

|November 5, 2016

Summary

Drug binding kinetics, not just affinity, predict drug effectiveness and safety. This review explores computational methods for quantitative structure-kinetics relationships (QSKR) in drug design.

More Related Videos

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR

Published on: November 29, 2014

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Published on: May 9, 2025

Related Experiment Videos

Last Updated: Mar 12, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry

Published on: September 13, 2014

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR

Published on: November 29, 2014

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Quantitative Structure-Activity Relationship, Activity Prediction, and Molecular Dynamics of Non-nucleotide Reverse Transcriptase Inhibitors

Published on: May 9, 2025

Area of Science:

Pharmacology
Computational Chemistry
Drug Discovery

Background:

Drug efficacy and safety are often predicted by binding affinity.
Kinetic properties offer additional critical insights but are less understood.
Quantitative structure-kinetics relationships (QSKR) are underexplored for modeling and ligand design.

Purpose of the Study:

To introduce the fundamental chemistry of drug binding kinetics.
To review recent advancements in computational tools for kinetic analysis.
To highlight applications of these tools in non-covalent binding kinetics.

Main Methods:

Fundamental chemical principles of binding kinetics.
Review of computational methodologies.
Case studies on non-covalent interactions.

Main Results:

Kinetics provide crucial differentiators for drug efficacy and safety.
Computational tools are advancing the understanding of QSKR.
These tools enable better prediction and design of drug candidates.

Conclusions:

Kinetic properties are vital for comprehensive drug assessment.
Computational approaches are key to unlocking QSKR insights.
Further development and application of these methods will enhance drug discovery.