So the portion of the protein within the core interacts via Vanderbilt forces we call London dispersion forces with the hydrocarbon tails of the phospholipids, these red structures shown in that diagram. Now, peripheral proteins, on the other hand, interact with the membrane less extensively. They don't have as much of that hydrophobic section to basically be able to interact in the same stabilizing way. 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.