Abstract
For membrane proteins, a bilayer environment has proven to be of fundamental importance for the isolation and stabilization of individual subunits and macromolecular complexes. For that reason, membrane protein reconstitution has long represented a biochemical challenge in the pursuit of biochemical, structural and functional studies. Protein-lipid nanodiscs offer a membrane-mimicking environment that provides many advantages for structural and functional studies of integral membrane proteins. In its original conception (Sliger’s lab), nanodisc formation requires that target membrane proteins of interest are purified in detergent and reconstituted into a bilayer disc, encapsulated by an amphipathic membrane scaffold protein (MSP).
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