When proteins undergo denaturation, which aspect of their structure is affected?

Denaturation of proteins specifically impacts the secondary, tertiary, and quaternary levels of structure. During this process, the strong covalent bonds that hold together the primary structure, which is the linear sequence of amino acids, remain intact. However, the levels of organization beyond this—where interactions such as hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals forces play crucial roles—are disrupted.

As conditions such as extreme pH, temperature changes, or exposure to certain chemicals alter the environment around the protein, the three-dimensional conformation can change dramatically. This can lead to a loss of functional structure, as the protein may unfold or aggregate. Consequently, it is the higher structural levels that are directly affected during denaturation.

Understanding this concept is vital in biochemistry because it illustrates how proteins can lose their functionality through changes in environment, underscoring the importance of structural integrity for biological activity.