protein-membrane interactions

The functional roles of lipid membranes is closely coupled to the function of the proteins that interact with them. Both the structural and dynamical properties of the bilayer environment have an effect on, and are affected by, the membrane-resident macromolecules (Fig. 1). For instance, even though it is not charged, cholesterol can increase the electrostatic binding of peripheral proteins to a membrane by virtue of its effects on lipid packing (and thus, surface charge density) and bilayer- and protein-hydration properties. Similarly, an ion channel can accelerate lipid flip-flop between leaflets as a result of the deformation of the membrane needed to minimize the exposure of hydrophobic moieties to water. A more recent example of a protein whose function is implicated in many physiological processes and which interacts with the membrane in a rather unique manner, is the human caveolin complex CAV1-8S. With a structure composed of 11 monomers resembling a sombrero, the protein likely sits within a single leaflet, displacing hudnreds of phospholipids while attracting cholesterol. Our research focuses on the mutual adaptation between CAV1-8S and the bilayer with a focus on combining computational and experimental techniques to probe relevant interactions and mechanisms at different resolution.