Journal article
Curvature elasticity and refolding of OmpA in large unilamellar vesicles
Publication Details
Authors: | Pocanschi, C.; Patel, G.; Marsh, D.; Kleinschmidt, J. |
Publication year: | 2006 |
Journal: | Biophysical Journal |
Pages range : | 75-77 |
Journal acronym: | Biophys. J. |
Volume number: | 91 |
ISSN: | 0006-3495 |
eISSN: | 1542-0086 |
DOI-Link der Erstveröffentlichung: |
Abstract
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.
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.
Keywords
149024-69-1 (OMPA outer membrane proteins), 18285-71-7 (1,2-dilauroylphosphatidylcholine), Bacterial Outer Membrane Proteins, Bacterial Outer Membrane Proteins/chemistry, Elasticity, Escherichia coli Proteins, Escherichia coli Proteins/chemistry, Liposomes, Liposomes, Phosphatidylcholines, Phosphatidylcholines/chemistry, Protein Folding
