Abstract
The lipid bilayer in a cell membrane serves as a natural solvent for membrane proteins. The physical principle of how the lipid bilayer mediates the folding, stability, and cooperativity between residues to facilitate the functions of membrane proteins in cells is not well understood. Here, we employed steric trapping as a tool to study membrane protein folding in a native lipid environment. This method couples spontaneous denaturation of a doubly biotinylated protein to the competitive binding of bulky monovalent streptavidin.
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