Related Experiment Video
Updated: Jun 8, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
Measurement of protein-ligand binding constants from reaction-diffusion concentration profiles
Yanhu Wei1, Paul J Wesson, Igor Kourkine
1Department of Chemical and Biological Engineering and Department of Chemistry, Northwestern University, 2145 Sheridan Road, Evanston, Illinois 60208, United States.
Abstract:
Protein-ligand dissociation constants, K(d), are determined precisely and down to the picomolar range from reaction-diffusion (RD) concentration profiles created by proteins diffusing through hydrogels functionalized with protein ligands. The RD process effectively amplifies the molecular-scale binding events into macroscopic patterns visible to the naked eye. The method is applicable to various protein-ligand pairs and does not require any prior knowledge about the protein structure.
Related Concept Videos
The Equilibrium Binding Constant and Binding Strength
The Equilibrium Binding Constant and Binding Strength
Protein-Drug Binding: Determination Methods
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...
Quantitative Aspects of Drug-Receptor Interaction
Complexation Equilibria: Overview
The equilibrium constant of the complexation reaction is represented as the formation constant...
Measuring Reaction Rates

