I have this question I need to answer and I am confused. I've checked my notes and book and can't find an answer. Here is the question: "Even though the beta barrel configuration for a transmembrane protein channel would seem an ideal channel, most of the channel proteins have multipass alpha helical domains. Why would this configuration be so well suited to membrane channels?" Is it just because the alpha helical proteins form a hole, where the inside is hydropholic and the exterior is hydrophobic (thus interacting with the phospholipids), and the hydrophilic interior makes it easier for the molecules to interact with the protein? I don't get why "beta barrell configuration would seem an ideal channel" in the first place. Confused here, lol.