Christoph A. Haselwandter, Rob Phillips
While modern structural biology has provided us with a rich and diverse picture of membrane proteins, the biological function of membrane proteins is often influenced by the mechanical properties of the surrounding lipid bilayer. Here we develop an analytic methodology connecting the hydrophobic shape of membrane proteins to the cooperative function of membrane proteins induced by bilayer-mediated elastic interactions. Application of this methodology to mechanosensitive channels shows that, in addition to protein separation and bilayer material properties, the sign and strength of elastic interactions, and associated cooperative gating characteristics, can depend on the protein shape and orientation. Our approach predicts how elastic interactions affect the molecular structure, organization, and biological function of proteins in crowded membranes.
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http://arxiv.org/abs/1209.3083
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