In fact, we have 123-4567 of these membrane spanning alpha helices. In fact, the predominant structure of transmembrane proteins inside our body actually consists of these membranespanic helices. Now, the thing about these membranespanic, alpha helices, is they consist predominantly of hydrophobic nonpolar amino acids. Why? Well, because these alpha helices that basically create this cylindrical structure that allows the movement of these h plus ions, they contain the hydrophobic nonpolar regions or amino acids because they want to be able to interact and stabilize, interact in a stabilizing way with the hydrophobic core, the red portion of that cell membrane. So we see that the structure of bacteria, or adoption consists largely of membrane spanning alpha helices that contain mostly nonpolar amino acids that can interact via nonpolar vanderviled interactions, lung dispersion forces with the hydrocarbon tails of these phospholipids.