An alpha-helix conformation is favored in the transmembrane domain of a membrane protein because:

Question

Quizplus · Accepted Answer

The intramolecular H-bonding that occurs between the amino and carboxyl groups stabilizes the alpha-helix conformation of the transmembrane domain. Additionally, within the hydrophobic core of the lipid bilayer, there are no other molecules which can form H-bonds and thus compete with the intramolecular H-bonds of the transmembrane peptide domain.

An Alpha-Helix Conformation Is Favored in the Transmembrane Domain of a Membrane