Related Experiment Video
Updated: Sep 27, 2026

Isothermal Titration Calorimetry for Measuring Macromolecule-Ligand Affinity
Published on: September 7, 2011
Applications of calorimetric methods to drug discovery and the study of protein interactions
Patricia C Weber1, F Raymond Salemme
13-Dimensional Pharmaceuticals Inc, 1020 Stony Hill Road, Yardley, PA 19067, USA.
Abstract:
Recent studies report the application of isothermal titration calorimetry and differential scanning calorimetry to the study of protein-ligand interactions, allosteric cooperativity and aspects of protein folding. New methods of data analysis compare alternative methods for determining ligand binding enthalpy and analyze potential sources of error in the experimental measurement of other thermodynamic parameters. Several reports examine issues concerning drug design and the correlation of thermodynamic and X-ray structural data. New instruments allow volumetric effects in biochemical systems to be evaluated calorimetrically and to substantially expand the throughput of differential scanning calorimetry measurements in drug discovery and other high-throughput applications.
Related Concept Videos
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...
The Equilibrium Binding Constant and Binding Strength
Protein Networks
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces
Drug Discovery: Overview
Applications Of NMR In Biology
The...

