Quantification of the effects of ionic strength, viscosity, and hydrophobicity on protein-ligand binding affinity.

ABSTRACT: In order to quantify the interactions between molecules of biological interest, the determination of the dissociation constant (K d) is essential. Estimation of the binding affinity in this way is routinely performed in "favorable" conditions for macromolecules. Crucial data for ligand-protein binding elucidation is mainly derived from techniques (e.g., macromolecular crystallography) that require the addition of high concentration of salts and/or other additives. In this study we have evaluated the effect of temperature, ionic strength, viscosity, and hydrophobicity on the K d of three previously characterized protein-ligand systems, based on variation in their binding sites, in order to provide insight into how these often overlooked unconventional circumstances impact binding affinity.

SUBMITTER: Papaneophytou CP 

PROVIDER: S-EPMC4137368 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature