Integral membrane proteins tend to be enriched for regular secondary structures in the transmembrane portions of their structures. Which statement explains this observation?

Question

Quizplus · Accepted Answer

Regular secondary structures, such as alpha-helices and beta-sheets, allow for the hydrogen-bonding potential of the backbone to be satisfied in a hydrophobic environment. This is because the backbone NH and C=O groups can form hydrogen bonds with each other, stabilizing the structure. This is important in the transmembrane domain of integral membrane proteins, where the environment is primarily hydrophobic due to the presence of the lipid bilayer.

Integral Membrane Proteins Tend to Be Enriched for Regular Secondary