help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Biophys. J. BioFAST: First Published August 4, 2006. doi:10.1529/biophysj.106.091439
© 2006 by the Biophysical Society.

A more recent version of this article appeared on October 15, 2006.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.106.091439v1
91/8/L75    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pocanschi, C. L.
Right arrow Articles by Kleinschmidt, J. H
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pocanschi, C. L.
Right arrow Articles by Kleinschmidt, J. H

BIOPHYSICAL LETTERS

Curvature elasticity and refolding of OmpA in large unilamellar vesicles

Cosmin L. Pocanschi 1, Geetika J. Patel 1, Derek Marsh 2* and Jörg H Kleinschmidt 1

1 University of Konstanz, Konstanz, Germany
2 Max-Planck-Institut für biophysikalische Chemie

* To whom correspondence should be addressed. E-mail: idreger{at}gwdg.de.

Submitted on June 16, 2006
Revised on July 15, 2006
Accepted on 1 August 2006


  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.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
N. K. Burgess, T. P. Dao, A. M. Stanley, and K. G. Fleming
{beta}-Barrel Proteins That Reside in the Escherichia coli Outer Membrane in Vivo Demonstrate Varied Folding Behavior in Vitro
J. Biol. Chem., September 26, 2008; 283(39): 26748 - 26758.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
D. Marsh
Lateral Pressure Profile, Spontaneous Curvature Frustration, and the Incorporation and Conformation of Proteins in Membranes
Biophys. J., December 1, 2007; 93(11): 3884 - 3899.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2006 by the Biophysical Society.