Analysis of Protein stability in ionic liquid by Differential Scanning Fluorimetry(DSF) (CAT#: STEM-MB-0755-WXH)

Introduction

Thermodynamic stability of proteins represents the free energy difference between the folded and unfolded protein states. This free energy difference is very sensitive to temperature, hence a change in temperature may result in unfolding or denaturation.
The interaction of ionic liquids with proteins adds a significant new landscape for the understanding of ionic-liquid solute interactions. With the vast range of cation and anion combinations available affording a differing balance of intermolecular interactions and thus interacting properties that can constitute an ionic liquid, not to mention mixtures of ions, the different anionic, cationic, hydrophobic, and polar interactions from each amino acid of a protein backbone becomes a many dimensional challenge.