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 URLanization, and biological function of proteins in crowded membranes.
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 explore the relation between the shape of membrane proteins and the cooperative function of membrane proteins induced by membrane-mediated elastic interactions. For the experimental model system of mechanosensitive ion channels we find that the sign and strength of elastic interactions depend on the protein shape , yielding distinct cooperative gating curves for distinct protein orientations . Our approach predicts how directional elastic interactions affect the molecular URLanization, and biological function of proteins in crowded membranes.
R
develop an analytic methodology connecting the hydrophobic
explore the relation between the
R
to
and
R
bilayer-mediated
membrane-mediated
R
Application of this methodology to mechanosensitive channels shows that , in addition to protein separation and bilayer material properties,
For the experimental model system of mechanosensitive ion channels we find that
D
, and associated cooperative gating characteristics, can
R
and orientation
, yielding distinct cooperative gating curves for distinct protein orientations
A
directional