title: Membrane defects accelerate outer membrane β-barrel protein folding.
abstract: Outer membrane β-barrel proteins spontaneously fold into lipid bilayers with rates of folding that are strongly influenced by the physical properties of the membrane. We show that folding is accelerated when the bilayer is at the phase transition temperature, because of the coexistence of lipid phase domains and the high degree of defects present at domain boundaries. These results are consistent with previous observations of faster folding into thin and highly curved membranes, which also contain a higher prevalence of defects. The importance of defects in β-barrel folding provides insight into the intrinsic folding process and the biological assembly pathway.
authors.affiliation: T. C. Jenkins Department of Biophysics, Johns Hopkins University , Baltimore, Maryland 21218, United States.
authors.forename: Emily J
authors.initials: EJ
authors.lastname: Danoff
authors.forename: Karen G
authors.initials: KG
authors.lastname: Fleming
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D006090:Gram-Negative Bacteria / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D044367:Phase Transition; D017510:Protein Folding; D017433:Protein Structure, Secondary; D044366:Transition Temperature
chemical_list: D001425:Bacterial Outer Membrane Proteins; D008051:Lipid Bilayers; C078167:OMPA outer membrane proteins