And so what they do is they instead use the polar sections to basically interact either with the polar heads of the phospholipids or the polar regions found on the surface of these integral proteins. And because the cell membrane, or generally the membrane, basically predominantly exists of the hydrophobic core, we see that the peripheral proteins cannot interact very well with the membrane. And so, due to these weaker interactions, peripheral proteins can readily dissociate from the membrane. In fact, when we'll discuss the signal transduction pathways and we'll look at G proteins, we'll see that G proteins are examples of these peripheral proteins, they can actually dissociate from that membrane and then go on and carry out some important type of process inside our body. So once again, integral proteins come in two types. We have transmembrane proteins that span the entire membrane, and we also have these integral proteins that only partially interact with that particular hydrophobic region.