Abstract
The fluid mosaic model had its origins in an analysis of the equilibrium thermodynamics of membrane systems, which led to the suggestion that the integral proteins of membranes are amphipathic molecules. This thermodynamic analysis continues to have considerable explanatory and predictive power for problems of membrane structure and function. In this paper, the analysis is applied to explain or predict the relatively hydrophobic amino acid composition of integral proteins, their large content of a-helical secondary structure, the characteristics of the short-range interactions of lipids and integral proteins, the molecular asymmetry of the integral proteins and phospholipids of membranes, the possible biogenesis of such asymmetry, and the mechanisms of transport of small ionic and polar molecules through membranes.
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