Related Experiment Video
Updated: Aug 21, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
The effects of neutral salts on the stability of macromolecules. A new approach using a protein-ligand binding system
Abstract:
A new approach to study the thermodynamics of salt-protein interaction is described using a protein-ligand binding system. The effects of salts on the thermodynamics of association or dissociation of the ligand are related to the effect on the hydrophobic side chains on the interior of the protein by these salts. The calculated free energies of transfer of a methylene group from an interior of the protein to salt solutions are +0.1, +0.06, -0.02, and -0.06 kcal/mol for Na2SO4, NaCl, NaSCN, and Cl3CCOONa at 1 M concentration, respectively. The relationships between the thermodynamic parameters and the partial molar entropies of the solutions are analyzed.
More Related Videos
Related Concept Videos
Metal-Ligand Bonds
In these complexes, transition metals form coordinate covalent bonds, a kind of Lewis acid-base interaction in which both of the electrons in the bond are contributed by a donor (Lewis base) to an electron acceptor (Lewis acid). The Lewis acid in...
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
Ionic Strength: Effects on Chemical Equilibria
In this solution, the primary cation—the calcium...
Complexation Equilibria: The Chelate Effect
Complexation Equilibria: Factors Influencing Stability of Complexes

