By Hugo O. Villar (Eds.)
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Extra info for Advances in Computational Biology
This finite-size scaling behavior at afirst-orderphase transition is qualitatively 34 MOURITSEN, SPEROTTO, RISBO, ZHANG, and ZUCKERMANN different from that of a continuous transition where, for example, the specific heat maximum diverges as C™^ ~ L^''^. Here a and v are the critical exponents characterizing the singularities of the specific heat and the correlation length, respectively. , from the position of the maximum in the specific heat, C(L), from the position of the maximum in the susceptibility, %(L), or from the criterion that the two minima in the free energy are equally deep.
6). hydrophobic contact interaction and the repulsive interaction due to a possible mismatch betv^een lipid bilayer and protein hydrophobic thicknesses. The results suggest that the formation of protein aggregates in the membrane plane is predominantly controlled by the strength of the direct van der Waals-like lipid-protein interaction. Whereas the mismatch is of prime importance for determining the phase equilibria, it is found that a mismatch may not be the only reason for protein aggregation within each of the individual phase.
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.