Pulse Proteolysis in Protein-Ligand Interactions

Abstract

Thermodynamic changes that occur when a protein and ligand bind may be used to better understand the nature and function of protein-ligand interactions. By establishing a method to detect thermodynamic changes, identifying proteins and the ligands in which they interact are valuable in understanding  the proteins involved in cellular functions and pharmacological mechanisms. Traditional methods that investigate protein stability such as circular dichroism and fluorospectrometry often require more biophysical instrumentation and a larger amount of proteins. However, pulse proteolysis later coupled with 2D gel electrophoresis provides an acceptable method for determining protein ligand interactions that minimizes the use of instruments and required samples. Later research demonstrates that the use of chromatography and SDS PAGE rather than 2D gel electrophoresis simplifies the process while still providing accurate experimental results.