The pair distribution functions have been measured from freeze-fracture pictures of bacteriorhodopsin and rhodopsin recombinants with diacyl phosphatidylcholines (PC) of various hydrocarbon chain lengths. Pictures were used of samples that had been frozen from above the phase transition temperature of the lipid. Measured functions were compared with those calculated from two model interparticle potential energy functions, (a) a hard-disk repulsion only, and (b) a hard-disk repulsion plus electrostatic repulsion for a point charge buried in the membrane. The measured functions for bacteriorhodopsin di 12:0 PC, di 14:0 PC, and di 16:0 PC recombinants can be simulated using an interparticle hard-disk repulsion only. Bleached rhodopsin di 12:0 PC and di 18:1 trans-PC recombinants, and dark-adapted rhodopsin di 10:0 PC recombinants yield functions that are better simulated by assuming an additional repulsive interaction. The measured functions resemble those calculated using the hard-disk plus electrostatic repulsion model. The picture of dark-adapted rhodopsin in di 18:1 trans-PC frozen from 20 degrees C shows partial aggregation that is apparent in the measured pair distribution function. This attractive interaction persists even at 37 degrees C, where the measured function shows deviations from the hard-disk repulsive model, indicative of an attractive interparticle interaction. Implications of these results are discussed in terms of protein-lipid interactions.

An expression is derived for the lipid-mediated intermolecular interaction between protein molecules embedded in a lipid bilayer. It is assumed that protein particles are accommodated by the bilayer, but they distort the lipids in some manner from their equilibrium protein-free configuration. We treat this situation by expanding the free energy density in the plane of the membrane as a Taylor series in some arbitrary parameter and its gradient. Minimization of the total membrane energy for a given particle configuration yields the interparticle interaction energy for that configuration. A test of the model is provided by measurement of the protein-protein pair distribution function from freeze-fracture micrographs of partially aggregated membranes. The measured functions can be simulated by adjustment of two parameters (a) a lipid correlation length that characterizes the distance over which a distortion of the bilayers is transmitted laterally through the bilayer, and (b) a term quantifying the energy of the protein-lipid interaction at the protein-lipid boundary. Correlation lengths obtained by fitting the calculated particle distribution functions to the data are found to be several nanometers. Protein-lipid interaction energies are of the order of a few kT.

We have studied the migration of the hindered phenol, octadecyl‐3,5‐bis (1,1‐dimethylethyl)‐4‐hydroxybenzenepropanoate, and the phosphite co‐stabilizer tris 2,4‐bis(1,1‐dimethylethyl)phenylphosphite, out of films of polypropylene (nominal melt flow 3.5 g/10 min). Loss of additive from an initial 10% weight‐% level in the polymer was followed by FTIR bands in the appropriate regions. Temperatures of 298 K, 313 K and 333 K were used. An attempt was made to analyze migration data using Fick's law for diffusion by means of a least squares fit. Octadecyl‐3,5‐bis (1.1‐dim ethylethyl)‐4‐hydroxybenzenepropanoate diffused according to Fick's law with a temperature independent diffusion constant (D = 1.27 × 10−15 m2 S−1) to a steady state concentration of 7.2 % + −0.56 weight‐%. The phosphite did not diffuse at all at 298 K and 313 K, but diffused with D = 8.1 × 10−16 m2 S−1 to a steady level at 333 K. Our interpretation of the phosphite migration data assumes that most of the phosphite in the sample is immobilized. A subset of the total phosphite level is free to diffuse to the surface of the polymer.

The effects of 9‐vinyl anthracene (VAn) on solution and emulsion polymerization of styrene are examined, to gain information about the mechanism of particle formation in emulsion polymerizations. Styrene solution polymerization in ethyl benzene is found to be inhibited by small amounts of VAn. In an emulsion system, the effects of VAn are found to depend on surfactant concentration [S]. With [S] = 0, addition of VAn engenders some inhibition and very little change in the steady‐state polymerization rate. As [S] is increased from zero to above the critical micelle concentration (cmc), a slight increases in the induction period and an increasing retardation (reduction in the steady‐state rate) are observed. Below the cmc, VAn has no significant effect on the particle number, but above the cmc it considerably increases the latter with concomitant appearance of very small (5–15 nm radius) particles. The data strongly support the supposition that the coagulative/homogeneous nucleation mechanism dominates particle formation for [S] below the cmc. Above the cmc, the data are compatible with both the micellar entry and coagulative/homogeneous mechanisms.

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