Final answer:
The Methionine (Met) residue in the hydrophobic core of T4 lysozyme helps to stabilize the protein's structure by promoting hydrophobic interactions. These interactions are crucial for maintaining the protein's tertiary structure.
Step-by-step explanation:
The Met residue buried within the folded hydrophobic core of T4 lysozyme plays a critical role in maintaining the protein's structure. Met, short for Methionine, is a hydrophobic amino acid. Its inclusion in the hydrophobic core of T4 lysozyme has the effect of stabilizing the hydrophobic core. This is because hydrophobic interactions are one of the main forces that contribute to the tertiary structure of a protein, alongside ionic bonding, hydrogen bonding, and disulfide linkages.
In the case of T4 lysozyme, Methionine's nonpolar side chain is conducive to maintaining the protein's complex three-dimensional structure by promoting the aggregation of hydrophobic R groups inside the protein. This organization leads to decreased hydrophobicity within the aqueous cellular environment and supports correct protein folding. Therefore, the Met residue helps in stabilizing the protein's structure by strengthening the hydrophobic interactions within the protein core.