Try it on paper first. A hint, the key idea and the worked solution are here when you need them.
Ravi boils an egg. The clear egg white turns solid and white, and it stays solid when the egg cools. His sister Tara adds lemon juice to warm milk, and white lumps appear.
Folding is driven by the hydrophobic effect and held by hydrogen bonds, salt bridges and disulphide bridges. Heat, pH, urea and thiols denature a protein, but its peptide bonds stay whole. The isoelectric point, pI, is the pH of zero net charge: the average of the two pK values on either side of the neutral form.
Have you tried it?
Work it out on paper first. It is fine to get stuck or make a mistake: that is how we learn. When you are ready, go through the solution one step at a time, and check each step against your own.
Step 1. The egg. Heat broke the weak bonds, so the albumin chains unfolded. Their exposed hydrophobic patches stuck to the patches of neighbouring chains, and the chains clumped into a solid network. Cooling does not undo this, because the chains are tangled together and cannot find their way back to the original fold.
Step 2. The milk. Casein has an isoelectric point near 4.6. At that pH its net charge is zero, so the molecules no longer repel each other. They clump and come out of solution as lumps.
Step 3. The bonds. No peptide bond was broken in either case. Heat and acid only upset the weak bonds and the charges, so the primary structure is intact.
Answer: The egg protein was denatured and aggregated, the milk protein clumped near its isoelectric point, and no peptide bonds broke.
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