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

Question

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 tend
to arrange themselves near the outside of the folded protein, where they can form hydrogen bonds with water and
with other polar molecules
2. 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 surrounding
water molecules.
3. Hydrophobic side chains form higrogen bonds with polar side chain inside a protein
4. Hydrophobic side chains tend to interact with water molecules inside a protein

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