On the inside side of the system, there are non-polar amino acids that can make bonds with the hydrophobic tails of the phospholipids found inside cell membrane structures.
An unusual combination of amino acids forms a channel protein, which embeds in the cell membrane and creates a hydrophilic channel for water and small, polar ions. Each channel protein, like all transport proteins, has a size and shape that keeps out all but the most particular molecules. A hydrophilic area forms in the core of the majority of channel proteins, which are composed of several similar protein subunits. Although the amino acids exposed within the hydrophobic cell membrane are hydrophilic on the inside, they are also non-polar. As a result, the protein is better able to bind to the membrane. Polar forces would drive the protein back into place if it tried to escape the membrane.
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