Researcher(s)
- Luke Coster, Biochemistry, University of Delaware
Faculty Mentor(s)
- Sharon Rozovsky, Chemistry and Biochemistry, University of Delaware
Abstract
Membrane proteins regulate key cellular processes and make up a large percentage of drug targets. If one wants to understand their function, then it is crucial to understand membrane proteins’ structure in native-like environments similar to biological membranes. Membrane proteins are commonly reconstituted in detergents for structural characterization. Since detergents are not structurally restricted, they can force the membrane protein into a non-native structure. To overcome this and still provide a native-like membrane environment, lipid nanodiscs are a desirable alternative for studying membrane proteins. Each lipid nanodisc is composed of a flat lipid bilayer disc encased by membrane scaffolding protein (MSP), a hydrophobic protein. Compared to detergents, lipid nanodiscs provide a more consistent size and composition of the hydrophobic environment, which structural and biochemical assays more reproducible and closer to native conditions. Here, I describe the preparation of lipid nanodiscs its characterization by biophysical techniques, and their use to study membrane proteins.