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goldbat748Lv1
28 Sep 2019
1. What is the purpose of boiling your protein samples before loading them into the polyacrylamide gel?
2. At the end of electrophoresis and Coomassie Blue Standing, would you expect a protein mixture to appear as a single protein band or as multiple protein bands in the polyacrylamide gel? Explain your reasoning.
3. GFP and BFP both consist of 238 amino acids, but differ in the identifies of two amino acids. Assume that both of these proteins have been denatured by boiling and denaturing solution, and are negatively charged from treatment with SDS.
Would you expect GFP and BFP to migrate the same distance during electrophoresis? Explain your reasoning.
1. What is the purpose of boiling your protein samples before loading them into the polyacrylamide gel?
2. At the end of electrophoresis and Coomassie Blue Standing, would you expect a protein mixture to appear as a single protein band or as multiple protein bands in the polyacrylamide gel? Explain your reasoning.
3. GFP and BFP both consist of 238 amino acids, but differ in the identifies of two amino acids. Assume that both of these proteins have been denatured by boiling and denaturing solution, and are negatively charged from treatment with SDS.
Would you expect GFP and BFP to migrate the same distance during electrophoresis? Explain your reasoning.
Jean KeelingLv2
28 Sep 2019
