At a higher pH, amino acids migrate towards which electrode during electrophoresis?

In an electrophoresis scenario, the movement of amino acids can be influenced significantly by their charge, which is determined by the pH of the environment. At a higher pH, the amino acids are more likely to be deprotonated, particularly at their amino and carboxyl groups. This means they may carry a net negative charge.

Electrophoresis operates on the principle that charged molecules move in an electric field. Positively charged molecules will migrate towards the cathode (the negative electrode) while negatively charged molecules will migrate towards the anode (the positive electrode).

When the pH is raised, it can lead to a situation where the carboxyl group of the amino acid loses a proton (becoming negatively charged) while the amino group may remain protonated, depending on the specific amino acid and its pKa values. At sufficiently high pH levels, the overall charge of many amino acids tends to be negative, making them migrate towards the positive anode due to the electric field.

Thus, if amino acids are predominantly negatively charged at a higher pH, they will move towards the positive anode, which is the correct outcome reflected in the choice. The characterization of movement in electrophoresis as related to charge