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The role of hydrophobic interaction in folding proteins into their tertiary and quaternary structure includes:1....

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The role of hydrophobic interaction in folding proteins into their tertiary and quaternary structure includes:1. The nonpolar (hydrophobic) side tend to cluster in the interior of the folded protein. In contrast, polar side chains tendto arrange themselves near the outside of the folded protein, where they can form hydrogen bonds with water andwith other polar molecules2. In an aqueous environment, hydrophobic molecules, including the nonpolar side chains of particular amino acids,tend to be forced together to minimize their disruptive effect on the hydrogen-bonded network of the surroundingwater molecules.3. Hydrophobic side chains form higrogen bonds with polar side chain inside a protein4. Hydrophobic side chains tend to interact with water molecules inside a protein

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