Ligand effects on protein thermodynamic stability
Related Experiment Video
Updated: Aug 7, 2026

Determination of Protein-ligand Interactions Using Differential Scanning Fluorimetry
Published on: September 13, 2014
1Departamento de Quimica Fisica, Campus Fuentenueva s/n, Universidad de Granada, 18071-Granada, Spain. sanchezr@ugr.es
Abstract:
A simple, partition-function formalism is used to describe the coupling between ligand binding and protein equilibrium unfolding. This general theoretical framework is shown to provide an adequate basis for the analysis of experimental ligand effects on the unfolding of complex protein systems. Nevertheless, the most important consequences of ligand binding for protein thermodynamic stability, as exposed by the partition-function approach, are found to be those demonstrated by Julian Sturtevant about 20 years ago.
More Related Videos
09:15Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
Published on: November 21, 2017
07:22How to Stabilize Protein: Stability Screens for Thermal Shift Assays and Nano Differential Scanning Fluorimetry in the Virus-X Project
Published on: February 11, 2019
Related Concept Videos
Ligand Binding Sites
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...
The Equilibrium Binding Constant and Binding Strength
The Equilibrium Binding Constant and Binding Strength
Cooperative Allosteric Transitions
Ligand Binding and Linkage
Complexation Equilibria: Factors Influencing Stability of Complexes