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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 22 (1993), S. 323-328 
    ISSN: 1432-1017
    Keywords: Lipid bilayer ; Binary mixture ; Lipidprotein interaction ; Lipid selectivity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract A model recently used to study lipid-protein interactions in one-component lipid bilayers (Sperotto and Mouritsen, 1991 a, b) has been extended in order to include two different lipid species characterized by different acyl-chain lengths. The model, which is a statistical mechanical lattice model, assumes that hydrophobic matching between lipid-bilayer hydrophobic thickness and hydrophobic length of the integral protein is an important aspect of the interactions. By means of Monte Carlo simulation techniques, the lateral distribution of the two lipid species near the hydrophobic protein-lipid interface in the fluid phase of the bilayer has been derived. The results indicate that there is a very structured and heterogeneous distribution of the two lipid species near the protein and that the protein-lipid interface is enriched in one of the lipid species. Out of equilibrium, the concentration profiles of the two lipid species away from the protein interface are found to develop a long-range oscillatory behavior. Such dynamic membrane heterogeneity may be of relevance for determining the physical factors involved in lipid specificity of protein function.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    European biophysics journal 19 (1991), S. 157-168 
    ISSN: 1432-1017
    Keywords: Lipid-protein interactions ; Phase transition ; Lipid bilayer ; Hydropobic thickness ; Protein aggregation ; Monte Carlo simulation ; Mean-field theory
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract Monte Carlo simulations and mean-field calculations have been applied to a statistical mechanical lattice model of lipid-protein interactions in membranes in order to investigate the phase equilibria as well as the state of aggregation of small integral membrane proteins in dipalmitoyl phosphatidylcholine bilayers. The model, which provides a detailed description of the pure lipid bilayer phase transition, incorporates hydrophobic matching between the lipid and protein hydrophobic thicknesses as a major contribution to the lipid-protein interactions. The model is analyzed in the regime of low protein concentration. It is found that a large mismatch between the lipid and protein hydrophobic thicknesses does not guarantee protein aggregation even though it strongly affects the phase behaviour. This result is consistent with experimental work (Lewis and Engelman 1983) considering the effect of lipid acyl-chain length on the planar organization of bacteriorhodopsin in fluid phospholipid bilayers. The model calculations predict that the lipid-mediated formation of protein aggregates in the membrane plane is mainly controlled by the strength of the direct lipid-protein hydrophobic attractive interaction but that direct protein-protein interactions are needed to induce substantial aggregation.
    Type of Medium: Electronic Resource
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