Which of the following scenarios best illustrates the process of protein denaturation and its impact on protein measurement methods?

Protein denaturation happens when a protein’s shape is disrupted, for example by heating, and the folded structure is lost, exposing hydrophobic parts that can stick together. This change can make standard assays, like the Bradford test, give lower readings because the dye no longer binds as it normally would. In contrast, a method that measures total nitrogen, such as Kjeldahl, will still detect the protein regardless of its shape. Thus, heating a protein sample and then measuring it with a dye‑based assay illustrates how denaturation alters the result. A quick example is boiling egg whites: the clear liquid becomes cloudy, and a Bradford test shows a much lower protein concentration than the actual amount.