Final answer:
Hydrophobic effects play a major role in the tertiary structure of proteins, including the formation of membrane-spanning alpha-helical domains in membrane proteins.
Step-by-step explanation:
Hydrophobic effects play a major role in the tertiary structure of proteins. The tertiary structure refers to the three-dimensional arrangement of a protein molecule, and it is determined by various chemical interactions, including hydrophobic interactions, ionic bonding, hydrogen bonding, and disulfide linkages.
Hydrophobic interactions occur when hydrophobic, or nonpolar, amino acid side chains cluster together in the interior of a protein, away from the surrounding aqueous environment. This clustering reduces the exposure of hydrophobic regions to water, minimizing the unfavorable disruption of water molecules.
One example of a protein structure where hydrophobic effects play a major role is the formation of membrane-spanning alpha-helical domains in membrane proteins. These hydrophobic domains allow the protein to interact with the hydrophobic interior of the lipid bilayer, anchoring it within the membrane.