Abstract
Over the years, there have been many developments and advances in the field of integral membrane protein research. As important pharmaceutical targets, it is paramount to understand the mechanisms of action that govern their structure–function relationships. However, the study of integral membrane proteins is still incredibly challenging, mostly due to their low expression and instability once extracted from the native biological membrane. Nevertheless, milligrams of pure, stable, and functional protein are always required for biochemical and structural studies. Many modern biophysical tools are available today that provide critical information regarding to the characterisation and behaviour of integral membrane proteins in solution. These biophysical approaches play an important role in both basic research and in early-stage drug discovery processes. In this review, it is not our objective to present a comprehensive list of all existing biophysical methods, but a selection of the most useful and easily applied to basic integral membrane protein research.
Highlights
It is estimated that today more than 50% of the marketed drugs target integral membrane proteins, mostly G-protein-coupled receptors (GPCRs), ion channels, and solute carrier transporters [4,5,6,7,8,9]
The study of structure–function relationships of membrane proteins has become paramount in the field of biomedical research and early drug discovery [12]
We present a small selection of methods, most of which can be implemented in any laboratory worldwide
Summary
Size exclusion chromatography multi-angle light scattering (SEC-MALS) is an accurate and versatile biophysical technique that is able to determine the composition, mass, and oligomeric state of membrane proteins in detergent solutions. An important study has been conducted that highlights the practicality of SEC-MALS in determining the oligomeric behaviour of membrane proteins in the presence of different detergents [61].
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