Question

where they execute important functions. The polypeptide chain of these proteins must cross the lipid bilayer. This presents a problem because the peptide bond is polar in nature. It turns out that in virtually all cases where an amino acid chain crosses a lipid bilayer it does so as an alpha helix. Suggest a reason why this is the case. (5 points)

Answer 1

In this case, it is likely that the polypeptide chain assumed an alpha helix configuration because the lipid bilayer did not have beta-barrel proteins.

Step-by-step explanation:

A polypeptide chain is naturally polar, however, a lipid bilayer is naturally non-polar. This makes it difficult and even prevents the polypeptide chain from crossing a lipid bilayer, since the composition of these two elements does not allow them to mix. In that case, the polypeptide chain has two options to take to successfully cross the lipid bilayer.

The first option that the polypeptide chain has is to allow the creation of twisted beta sheets in the shape of a closed barrel in its structure. This only works if the lipid bilayer has beta barrel proteins in its composition to act as a transport channel for the polypeptide chain. However, few lipid layers have this protein.

Most likely, the polypeptide chain assumes an alpha helix conformation to cross lipid bilayers that do not have beta-barrel proteins. By assuming the beta conformation, the polypeptide chain reinforces the hydrogen bonds present in its composition, allowing it to cross the lipid bilayer without having its conformation and structure disassembled.