Abstract
Integral membrane proteins (IMPs) play crucial roles in all cells and represent attractive pharmacological targets. However, functional and structural studies of IMPs are hindered by their hydrophobic nature and the fact that they are generally unstable following extraction from their native membrane environment using detergents. Here, we devised a general strategy for in vivo solubilization of IMPs in a functional conformation without the need for detergents or mutations to the IMP itself. This technique, called SIMPLEx (solubilization of IMPs with high levels of expression), involves creating fusions between an IMP target and truncated apolipoprotein A-I, which serves as an amphipathic proteic “shield” that sequesters the IMP from water and promotes its solubilization.
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