Protein lateral distribution in lipid bilayer membranes

We analyse recent ESR measurements on Ca²⁺ ATPase and Myelin proteolipid apoprotein reconstituted in phosphatidylcholine bilayer membranes. Our intention is to discover whether the measurements indicate significant protein-protein repulsive or attractive interactions. In order to do so we have studied a model of a lipid bilayer membrane containing transbilayer proteins. It represents the proteins by hexagons moving on a triangular lattice interacting via an energy E ₀ which can be attractive, repulsive or zero. The last-named represents the random case studied earlier. We find that all of the Ca²⁺ ATPase data is best described either by the random model or one in which there is always at least one layer of lipid chains between every pair of proteins. We find that all of the Myelin PLA data is best described by a random distribution of hexamers and not by an annulus model of hexamers. We suggest measurements that can be done in order to unambiguously settle the question of whether these systems are best described by a random-type model or an annulus-type model.Abbreviations PC phosphatidylcholine - DMPC dimyristoyl PC - DPPC dipalmitoyl PC - EYPC egg yolk PC - 14-PCSL 1-acyl-2-14-(4,4-dimethyloxazolidine-N-oxyl)steroyl]-sn-glycero-3-phosphocholine - DPH 1,6-diphenyl-1,3,5-hexatriene - PLA proteolipid apoprotein - ESR electron spin resonance - T _c temperature of main lipid phase transition Work supported by NSERC of Canada