Which mechanism initiates protein misfolding when hydrophobic amino acid side chains are exposed to aqueous solvent?

💡 Explanation

When hydrophobic side chains are exposed to aqueous solvent, the hydrophobic effect occurs because water molecules form ordered cages, decreasing entropy globally. This drives the protein to minimize exposed hydrophobic area, leading to aggregation or misfolding. Therefore increased entropy of water occurs rather than disulfide disruption, charge repulsion, or alpha-helix destabilization, which rely on different local chemical mechanisms.

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