Which of the following is TRUE regarding protein folding into a native structure?

The statement that hydrophobic residues are buried to remove themselves from water is accurate in the context of protein folding and achieving a native conformation. Proteins have a complex three-dimensional structure that forms through folding, driven primarily by the chemical properties of their amino acid side chains.

Hydrophobic (or non-polar) residues tend to avoid contact with water due to their inability to form favorable interactions with water molecules. When a protein folds, these hydrophobic residues are typically found in the interior of the protein structure, away from the aqueous environment. This arrangement stabilizes the protein's structure through hydrophobic interactions, which contribute significantly to the overall stability and proper functioning of the protein.

In contrast, hydrophilic (or polar and charged) residues are often located on the exterior of the protein, interacting favorably with the surrounding water molecules. This organization of residues—buried hydrophobic segments and exposed hydrophilic regions—maximizes thermodynamic stability and ensures that the protein can effectively perform its biological functions. Therefore, the observation of hydrophobic residues being sequestered within the protein structure is a fundamental principle in understanding protein folding.