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Phys. Rev. Lett. 101, 128104 (2008) [4 pages]

Cluster Formation of Transmembrane Proteins Due to Hydrophobic Mismatching

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Ulrich Schmidt, Gernot Guigas, and Matthias Weiss
Cellular Biophysics Group (BIOMS), German Cancer Research Center, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany

Received 26 March 2008; published 19 September 2008

Membranes are the defining envelopes of living cells. At this boundary a multitude of transmembrane proteins mediate signal and mass transfer between cells and their environment. Clustering of these proteins is a frequent and often vital phenomenon that relies at least in part on membrane-mediated interactions. Indeed, the mismatch between proteins’ hydrophobic transmembrane domains and the surrounding lipid bilayer has been predicted to facilitate clustering, yet unequivocal quantitative data in support of these predictions have been lacking. Here, we have used coarse-grained membrane simulations to thoroughly address the clustering of transmembrane proteins in detail. Our results emphasize the universal nature of membrane-mediated attraction which relaxes the need for a plethora of fine-tuned interactions between membrane proteins.

© 2008 The American Physical Society

URL:
http://link.aps.org/doi/10.1103/PhysRevLett.101.128104
DOI:
10.1103/PhysRevLett.101.128104
PACS:
87.15.kt, 87.16.A−, 87.16.D−

See Also

Comment: Frédérick de Meyer and Berend Smit, Comment on “Cluster Formation of Transmembrane Proteins Due to Hydrophobic Mismatching”, Phys. Rev. Lett. 102, 219801 (2009).

Reply: Ulrich Schmidt, Gernot Guigas, and Matthias Weiss, Schmidt, Guigas, and Weiss Reply:, Phys. Rev. Lett. 102, 219802 (2009).