Curvature elasticity and refolding of OmpA in large unilamellar vesicles.
The stability of OmpA in large unilamellar vesicles of dilauroyl phosphatidylcholine was studied using different concentrations of urea. The effective energy of unfolding, as determined from refolding experiments, is greater than that for small sonicated unilamellar vesicles by an amount that is compatible with estimates of the elastic energy of highly curved vesicles. The on-rate for refolding and insertion is slower for large unilamellar vesicles than for small unilamellar vesicles, which indicates a contribution of vesicle strain also to the free energy of the transition state.
Pocanschi
Cosmin L
CL
Patel
Geetika J
GJ
Marsh
Derek
D
Kleinschmidt
Jörg H
JH
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004548:Elasticity; D029968:Escherichia coli Proteins / Q000737:chemistry; D008081:Liposomes; D010713:Phosphatidylcholines / Q000737:chemistry*; D017510:Protein Folding
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D008081:Liposomes; D010713:Phosphatidylcholines; C078167:OMPA outer membrane proteins; C015153:1,2-dilauroylphosphatidylcholine