Consequences of Disrupted Hydrophobic Interactions

Amino acids are the building blocks of proteins and serve various roles in biological functions. Each amino acid has a unique side chain ( extit{R group}) that determines its chemical properties and influences protein structure and function. For instance, hydrophobic amino acids tend to cluster in the interior of proteins, while hydrophilic ones are often found on the surface. The primary structure of a protein is the linear sequence of amino acids, while higher-order structures are shaped by various interactions, including hydrogen bonds, ionic bonds, and hydrophobic interactions.

Consider an experiment where a researcher is studying the effects of temperate changes on a specific protein's structure. The protein consists of 200 amino acids, of which 20 are phenylalanine residues. Phenylalanine is a nonpolar aromatic amino acid. The researcher discovers that an increase in temperature leads to the disruption of hydrophobic interactions within the protein's tertiary structure. What is the most likely consequence of this disruption?