Final answer:
The interior of channel proteins is usually lined with polar and charged amino acids, which interact with the aqueous environment inside the channel. Non-polar amino acids are typically found on the exterior of membrane proteins, interacting with the hydrophobic core of the lipid bilayer.
Step-by-step explanation:
The channel protein interior is generally lined by polar and charged amino acids. This is because the interior of channel proteins is typically aqueous, meaning they will be in contact with water molecules passing through the channel. Polar or charged amino acids are hydrophilic, meaning they can interact favourably with water, which is crucial for the function of the channel in a cellular membrane.
On the other hand, the exterior of membrane-embedded proteins, which are in contact with the fatty acid tails of the phospholipid bilayer, will primarily consist of non-polar amino acids. These non-polar amino acids are hydrophobic and interact well with the hydrophobic core of the membrane, thus helping to anchor the protein within the membrane.
These differences in amino acid composition are essential for the proper folding and function of proteins in different cellular environments. For example, soluble proteins that are not associated with membranes typically have nonpolar amino acids on the interior and polar amino acids on the surface, the opposite of what is observed in membrane proteins.