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Membrane Elastic Fluctuations and the Insertion and Tilt of ß-Barrel Proteins

Derek Marsh ^*, Baladhandapani Shanmugavadivu  and Jörg H. Kleinschmidt 

^* Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, Göttingen, Germany; and University of Konstanz, Fachbereich Biologie, Konstanz, Germany

Correspondence: Address reprint requests to Derek Marsh, Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, 37070 Göttingen, Germany. Tel.: 49-551-201-1285; Fax: 49-551-201-1501; E-mail: dmarsh{at}gwdg.de or Jörg H. Kleinschmidt, University of Konstanz, Fachbereich Biologie, 78547 Konstanz, Germany. Tel.: 49-7531-88-3360; Fax: 49-7531-88-3183; E-mail: joerg.helmut.kleinschmidt{at}uni-konstanz.de.

Folding of porin-like ß-barrel outer membrane proteins can be achieved in the presence of phospholipid vesicles, and takes place concurrently with incorporation into the membrane. The pronounced dependence found for the insertion of the protein OmpA on membrane thickness (Kleinschmidt, J. H., and L. K. Tamm. 2002. J. Mol. Biol. 324:319–330) is analyzed in terms of the effects of out-of-plane elastic fluctuations on the area dilation modulus (Evans, E., and W. Rawicz. 1990. Phys. Rev. Lett. 64:2094–2097). For unstrained large unilamellar vesicles, the elastic free energy for membrane insertion is predicted to depend on the fourth power of the membrane thickness. The influence of thermally induced bending fluctuations on the effective tilt of the OmpA ß-barrel in disaturated phosphatidylcholine membranes of different thicknesses (Ramakrishnan, M., J. Qu, C. L. Pocanschi, J. H. Kleinschmidt, and D. Marsh. 2005. Biochemistry. 44:3515–3523) is also considered. A contribution to the orientational order parameter that scales as the inverse second power of the membrane thickness is predicted.

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