1. Why are proteins treated with ionic detergent (SDS), reducing agents
(DTT), and heat before SDS-PAGE?
2. Why do SDS-coated proteins migrate in an electric field?
3. What is the purpose of using experimental controls?
4. Name four of the main ingredients of the Laemmli sample buffer. What does
each do?
5. Why is it important to denature proteins before electrophoresis?
6. What is the difference between the primary and quaternary structures of
proteins?
7. What is the optimal temperature for denaturing your protein? Would
freezing work?
8. Is there an optimal time to incubate your sample at 95°C?
9. Is there a difference between using Laemmli buffer with and without
dithiothreitol (DTT)?
10. What happens if you use a higher or lower concentration of
Tris/glycine/SDS (TGS) running buffer?