By Hugo O. Villar (Eds.)
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By focusing on a model without direct protein-protein interactions we have therefore managed to isolate the effects of purely lipid-facilitated protein aggregation. It is important to know the nature of these effects before more realistic and complicated models involving long-range, direct, protein-protein interactions are invoked. D. Compositional Lipid Profiles in Binary Lipid Mixtures Near a Protein Wall We now consider the next level of complexity where a large protein is embedded in a lipid bilayer composed of two different lipid species, A and B.
The full finite-size scaling behavior of C(T) is shown in Figure 6(b). The expected scaling behavior for a first-order phase transition is clearly confirmed by this figure. The equilibrium phase transition temperature can be estimated from these data. , 1992a). Experimentally, it is virtually Figure 5. Mismatch model of the main phase transition in DPPC bilayers; cf. Eq. (3). F(TmiL)), in the free energy functional at the transition for mismatch values (from bottom to top) TA = 3 (no transition), 4 (critical point), and 5 (first-order transition) as a function of linear lattice size, L TA is in units of x10"^^ erg/A.
It specifically suggests that the direct lipid-polypeptide interactions are responsible for the location of the critical mixing point. Figure 10(b) shows a comparison between the computer simulation results and the experimental data for the enthalpy of melting, A^, as a function of peptide concentration. B. Lipid-Acyl-Chain Order-Parameter Profiles Near Small Proteins The question of the shape and the coherence length of the acyl-chain order parameter near integral membrane proteins was originally addressed within the conventional Landau-de Gennes theory (Abney and Owicki, 1985).