Protein-induced membrane asymmetry modulates OMP folding kinetics and stability.

ABSTRACT: Biological membranes are asymmetric structures, with asymmetry arising from differences in lipid identity in each leaflet of the bilayer, as well as non-uniform distribution of lipids and small molecules in the membrane. Proteins can also induce and modulate membrane asymmetry based on their shape, sequence and interactions with lipids. How membrane asymmetry affects macromolecular behaviour is poorly understood because of the complexity of natural membrane systems, and difficulties in creating relevant asymmetric bilayer systems in vitro. Here, we present a method exploiting the efficient, unidirectional folding of the transmembrane β-barrel outer membrane protein, OmpA, to create asymmetric proteoliposomes with protein-induced dipoles of known direction (arising from sequence vari

SUBMITTER: Machin JM 

PROVIDER: S-EPMC12060775 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature