Chromatographic techniques and their application to studies of conformational changes, stability and refolding of proteins

 

K. Mayolo-Deloisa, L.M. Martínez and M. Rito-Palomares

 

 

The increase in protein applications in various fields; such as medicine, environmental protection and food industry; has generated a special interest in the development of processes for the analyses and purification of proteins. Liquid chromatography has been widely exploited to carry out such analyses because of its versatility. The resolution of protein mixtures by liquid chromatography is based upon specific conditions, in which solutes dissolved in a mobile phase interact with a stationary phase. Depending upon the chemical nature of the type of interactions, there are different chromatographic techniques. This review paper includes the basic principles and main characteristics of the liquid chromatographies used in the analysis of proteins, such as: size exclusion, ion exchange, hydrophobic interaction and reverse phase. Moreover, it shows the applications of such techniques in the study of conformational changes, stability and refolding of proteins. Such research fields have raised attention from research groups in the last decade.