Statistical mechanics of lipid membranes. Protein correlation functions and lipid ordering.
An expression is derived for the lipid-mediated intermolecular interaction between protein molecules embedded in a lipid bilayer. It is assumed that protein particles are accommodated by the bilayer, but they distort the lipids in some manner from their equilibrium protein-free configuration. We treat this situation by expanding the free energy density in the plane of the membrane as a Taylor series in some arbitrary parameter and its gradient. Minimization of the total membrane energy for a given particle configuration yields the interparticle interaction energy for that configuration. A test of the model is provided by measurement of the protein-protein pair distribution function from freeze-fracture micrographs of partially aggregated membranes. The measured functions can be simulated by adjustment of two parameters (a) a lipid correlation length that characterizes the distance over which a distortion of the bilayers is transmitted laterally through the bilayer, and (b) a term quantifying the energy of the protein-lipid interaction at the protein-lipid boundary. Correlation lengths obtained by fitting the calculated particle distribution functions to the data are found to be several nanometers. Protein-lipid interaction energies are of the order of a few kT.
D055592:Biophysical Phenomena; D001703:Biophysics; D008081:Liposomes; D008563:Membrane Lipids; D008565:Membrane Proteins; D008954:Models, Biological; D013223:Statistics as Topic; D013816:Thermodynamics
D008081:Liposomes; D008563:Membrane Lipids; D008565:Membrane Proteins