Try it on paper first. A hint, the key idea and the worked solution are here when you need them.
Glutamic acid has pK values 2.2 (carboxyl group), 4.3 (acidic side chain) and 9.7 (amino group). Histidine has pK values 1.8 (carboxyl group), 6.0 (basic side chain) and 9.2 (amino group).
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. Glutamic acid. The neutral form lies between the two acid pK values, 2.2 and 4.3. So .
Step 2. Histidine. The neutral form lies between the two basic pK values, 6.0 and 9.2. So .
Step 3. The field. At pH 7.0 glutamic acid is above its pI, so it is negative and moves towards the positive electrode. Histidine is a little below its pI, so it is weakly positive and moves slowly towards the negative electrode.
Answer: 3.25 and 7.6; glutamic acid goes to the positive electrode and histidine to the negative one.
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