Q
how to do titration curves of amino acids
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Titration curves of amino acids involve gradually adding a titrant to an amino acid solution and measuring the pH change. Each amino acid has at least two titratable groups: the amino (–NH3+) and carboxyl (–COOH) groups. Some, like histidine, have additional ionizable side chains. Start by dissolving the amino acid in water to create a solution with known concentration. Adjust the pH to a starting point, then titrate with a strong acid (like HCl) or base (like NaOH), depending on the initial pH. As you add the titrant, record the pH at regular intervals. Plotting these pH values against the volume of titrant added generates the titration curve. Key points on this curve include the pKa values of the titratable groups, visible as regions where the pH changes less rapidly. These correspond to the points where 50% of the molecules have lost or gained a proton. The curve will reveal the isoelectric point (pI) — the pH at which the amino acid exists primarily in its zwitterion form, with equal positive and negative charges.
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