What is the role of hydrophobic interactions in protein folding. Differentiate between the tertiary and quaternary structures of proteins.

Hydrophobic interactions play a crucial role in protein folding by driving the packing of nonpolar amino acid side chains in the interior of the protein structure. When a protein folds, the hydrophobic residues tend to move away from the aqueous environment and cluster together in the protein's core, minimizing their contact with water molecules. This is _____ ________ _______ _________ __________ _______ ______ ________ _______ ________ _________.
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