Cluster formation of transmembrane proteins due to hydrophobic mismatching

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.