What is the correct sequence of events leading to protein denaturation when bovine albumin is exposed to extreme pH levels?

When bovine albumin is placed in a solution with a very high or very low pH, the hydrogen ions (H⁺) or hydroxide ions (OH⁻) flood the protein and compete for the ionizable side chains, disrupting the normal salt bridges and hydrogen bonds that hold its three‑dimensional shape. This ionic assault causes the protein’s backbone to lose its regular hydrogen‑bonding pattern, so the alpha‑helices and beta‑sheets unravel. As the secondary structure collapses, the hydrophobic core is exposed and the protein’s tertiary contacts break, leading to a random coil configuration. The unfolded chains then aggregate or precipitate because they can no longer maintain their native conformation. For example, if albumin is shifted to pH 2, the excess protons protonate acidic residues, breaking the salt bridges that keep the protein folded, and the protein finally flattens into a disordered shape.