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Bio Lab Skills
PAGE Quiz Questions
| Question | Answer |
|---|---|
| What chemical in the loading buffer provides density so the sample sinks into the well? | Glycerol |
| Why are protein samples heated at 95°C before electrophoresis? | denature proteins |
| What would happen if a student forgot to add beta-mercaptoethanol to the sample? | Disulfide bonds would remain intact, so some proteins would not fully linearize. |
| A gel was allowed to run until the Bromophenol Blue band completely exited. What is the most likely outcome | Some proteins may run out the gel and be lost. |
| What is the main difference between Native-PAGE and SDS-PAGE? | Proteins remain folded and intact in Native-PAGE. |
| Which properties affect protein migration in Native-PAGE? | charge density, size (#of Amino acids), and shape |
| Two proteins have identical molecular weights. In Native-PAGE, protein A is globular and protein B is elongated. Which migrates faster? | protein A |
| Why is polyacrylamide gel used instead of agarose for protein separation? | smaller pore size suitable for proteins |
| Which of the following is a limitation of Native-PAGE? | cannot determine accurate molecular weight |
| A protein shows three bands in a Native-PAGE run, but only one band in SDS-PAGE. What does this suggest? | protein exist in multiple oligomeric forms |
| You need to preserve enzyme activity while separating proteins by electrophoresis. Which approach is best? | Native-PAGE without SDS |