Methods in Studying Proteins

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Thought Questions

1. What are the advantages of 2D-PAGE compared to that of isoelectric focusing or SDS-PAGE? 

2. What situations would be more suitable to use native PAGE rather than SDS-PAGE? 

3. Why would changing the buffer pH affect the migration of proteins through PAGE? 

4. Why would certain changes in amino acid composition in proteins affect their migration through PAGE? 

5. How would changing amino acid composition affect the elution of proteins in size exclusion chromatography, ion exchange chromatography, and affinity chromatography? 

6. What will be the difference in parameters when an anion exchanger and a cation exchanger are both used to separate the same mixture of proteins? 

7. What other known ligand-ligand interactions can be used for protein purification? 

8. Why is proline a difficult amino acid to work with in determining the amino acid sequence using enzymes or chemicals? 

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◄ Protein Isolation and Purification Workflow
📚 Reading Module: Techniques in Protein Isolation and Characterization ►