Membrane proteins represent more than 60 percent of all drug targets. As such, an understanding of the structure-function relationship of membrane proteins is critical to the discovery and development of new pharmaceuticals. Due to the hydrophobic nature of the residues in the membrane spanning portion of the protein, membrane proteins are typically inactive and structurally unstable in the absence of the lipid membrane.
Therefore, successful solubilisation of membrane proteins in surfactant micelles and other stabilizing systems such as nanodiscs is critical for in vitro studies of receptor function, structure, and activity.
Malvern solutions within the field of membrane protein characterization include:
- Optimization of protein detergent complex solution conditions using triple detection SEC, including quantification of both free and bound surfactants.
- Characterization of the detergent CMC and the micelle size using dynamic light scattering.
- Measurement of the second virial coefficient, used to optimize the thermodynamic conditions for crystal formation, with static light scattering, both batch and SEC coupled.