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The channel loses its ionic conductivity when it dissociates into monomeric units. Studies of the statistics of channel opening by conductance measurements Computation of Lipid-Protein Interactions 27 show that the dimers (channels) and monomers are in thermal equilibrium (Hladky and Haydon, 1972; Bamberg and Laiiger, 1973; Zingsheim and Neher, 1974) G+G^G2 (7) where G and G2 represent the gramicidin monomers and dimers, respectively. , 1983). 7 A. This is consistent with the fact that a decrease in mismatch makes the dimeric state more stable.

The fundamental problem in numerical investigations of cooperative phenomena is associated with an unambiguous assessment of the nature of phase transitions as well as a determination of the precise location of the phase boundaries in a phase diagram. Numerical simulations share this problem with laboratory experiments. The root of the problem is that most approaches do not function on the level of the free energy but rather in terms of derivatives of the free energy, such as densities and order parameters (first derivatives) or response functions (second derivatives).

Transient oscillatory behavior of the lipid concentration profiles, P{r), for an equimolar mixture of DMPC and DSPC, as a function of the distance, r, from a very large integral membrane protein of hydrophobic length dp = 26A. The data are obtained from computer simulations on a system with 60 x 60 lipid chains and refer to a temperature, 7= 325 K. nature of the results for static proteins that the structured concentration profiles in Figure 15 will facilitate a medium-range, lipid-mediated, indirect, protein-protein attraction which will influence the state of protein aggregation.

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