Regensburg 2013 – scientific programme

Parts | Days | Selection | Search | Updates | Downloads | Help

BP: Fachverband Biologische Physik

BP 18: Membranes and Vesicles I

BP 18.5: Talk

Wednesday, March 13, 2013, 10:45–11:00, H44

Shape determines membrane protein cluster formation — Diana Morozova, Matthias Weiss, and •Gernot Guigas — Experimental Physics I, University of Bayreuth

About 30% of all protein species in a cell are membrane proteins. They take part in a multitude of vital cellular processes, e.g. signal and mass transfer at the plasma membrane. In many cases, membrane proteins need to cluster to perform their specific duty. Using mesoscopic simulations, we have studied the influence of protein shape on the clustering ability. We show via the potential of mean force that lipid-mediated interactions between transmembrane proteins depend on two key parameters [1]: the shape of the proteins' hydrophobic domain and their hydrophobic mismatch. Protein interactions can be attractive or repulsive, depending on the characteristic bilayer perturbations induced by the proteins. These findings are compared to results on peripheral membrane proteins that reside only in one leaflet of the membrane [2]. Here, we observe various higher-order structures depending on the size and penetration depth of the protein's hydrophobic moiety. Surprisingly, even clustering across opposing leaflets of a bilayer is observed.

[1] D. Morozova, M. Weiss, and G. Guigas, Soft Matt. 8, 11905 (2012). [2] D. Morozova, G. Guigas, and M. Weiss, PLOS Comp. Biol. 7, e1002067 (2011).