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Biochemistry · Biomolecules and enzymes: hydrophobic effect in folding
Sample itemIn a water-soluble globular protein, nonpolar side chains such as leucine, isoleucine and phenylalanine are mostly buried in the interior. Which force chiefly drives this arrangement?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
B. The hydrophobic effect, increasing entropy of surrounding water
Burying nonpolar side chains releases ordered water molecules that surrounded them, raising the entropy of the solvent. This hydrophobic effect is the main driving force of folding, while hydrogen bonds, ionic bonds and disulfides refine and stabilise the structure.
Option by option
A. Ionic bonds between buried acidic and basic residues
Ionic interactions occur between charged residues, mostly at the surface, and do not explain burial of nonpolar chains.
B. The hydrophobic effect, increasing entropy of surrounding water (correct)
Correct. Burying nonpolar groups frees ordered water, and the resulting entropy gain drives folding.
C. Covalent cross-linking of the buried side chains
Covalent cross-links such as disulfides involve cysteine and do not hold leucine or isoleucine in the core.
D. Hydrogen bonding of every buried residue to water
The buried residues are nonpolar and cannot hydrogen bond with water, which is exactly why they leave the aqueous phase.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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