A model of the plasma membrane showing several biological molecules, including a transmembrane protein, is shown in Figure 1.

The figure shows a diagram of a phospholipid bilayer with an embedded transmembrane protein. The protein is coiled into a helical shape where it is buried between the membrane lipids. Polar areas of the protein are labeled on the portions of the protein that stick out from the two membrane surfaces. Nonpolar areas of the protein are labeled on the coiled portion that is buried between the membrane lipids.

Figure 1. Phospholipid bilayer with transmembrane protein

Which statement best explains why correct protein folding is critical in the transmembrane protein shown above?

Question

A model of the plasma membrane showing several biological molecules, including a transmembrane protein, is shown in Figure 1.

The figure shows a diagram of a phospholipid bilayer with an embedded transmembrane protein. The protein is coiled into a helical shape where it is buried between the membrane lipids. Polar areas of the protein are labeled on the portions of the protein that stick out from the two membrane surfaces. Nonpolar areas of the protein are labeled on the coiled portion that is buried between the membrane lipids.

Figure 1. Phospholipid bilayer with transmembrane protein

Which statement best explains why correct protein folding is critical in the transmembrane protein shown above?

BlackTom AI · Accepted Answer

First, restate the scenario: a transmembrane protein spans a phospholipid bilayer, with polar regions outside the membrane surfaces and nonpolar regions buried within the hydrophobic core of the bilayer. The question asks why correct protein folding is critical for this transmembrane protein.
Option 1 suggests that quaternary structure interactions increase hydrogen bonding in the membrane and reduce fluidity. While protein folding can influence interactions, the primary determinant for spanning the membrane is the distribution of hydrophobic and hydrophilic residues along the protein, not quaternary hydrogen bonding to rigidify the membrane itself. Also, quaternary structure is about subunit assembly, which is not the central factor in anchoring a single transmembrane helix within a lipid bilayer.
Option 2 states that interactions of the peptide bonds with the membrane affect the rate of substance crossing. Peptide bonds themselves are relatively rigid backbones and do not directly govern selective transport across the bilayer; rather, the embedment and orientation of amino acid side chains (hydrophobic vs hydrophilic) determine anchoring and permeability characteristics. This option misattributes the mechanism, focusing on peptide bonds rather than side-chain properties.
Option 3 claims that interactions of the hydrophobic and hydrophilic amino acids help to anchor the protein in the membrane. This aligns with the fundamental principle that transmembrane regions are rich in hydrophobic residues that favor the lipid bilayer interior, while polar or charged residues are exposed to aqueous environments at the membrane surfaces. The alternating distribution of hydrophobic and hydrophilic regions drives proper spanning orientation and stable anchoring, enabling the protein to maintain its functional conformation within the membrane.
Option 4 proposes that interactions between the protein and phospholipids increase membrane fluidity. In reality, the embedded protein typically stabilizes specific regions or orientations within the bilayer rather than universally increasing fluidity; while protein-lipid interactions can influence local dynamics, the dominant idea here is about correct folding and residue alignment enabling anchoring, not broad enhancement of membrane fluidity.
In summary, the key idea is that the correct folding places hydrophobic residues in the membrane interior and exposes hydrophilic residues to the aqueous surfaces, thereby anchoring the protein in place. The other options either misattribute the mechanism (focusing on peptide bonds or quaternary structure) or misstate the effect on membrane properties (fluidity) rather than anchoring and proper orientation.

APBIO141-031 with labs Unit 5 Test

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