6. Asparagine and glutamine residues in proteins will sometimes be deamidated in

Question

6. Asparagine and glutamine residues in proteins will sometimes be deamidated into aspartic acid and glutamic acid, respectively. If this happens to a purified protein, it will result in a mixed population of proteins with the original Asn and Gln resides and proteins in which they have been replaced by Asp and Glu. What would be the best technique to separate original wild-type proteins from the deamidated ones? A) SDS-PAGE B) Solubility assays (salting out) E) Gel filtration D) lon exchange Extra credit 2: Would the pl of the deamidated protein be higher, the same, or lower compared to that of the wild-type protein?

Explanation / Answer

Aspartic acid (Asp, D) and glutamic acid (Glu, E) are negatively charged. Asparagine and glutamine are polar amino acids.

The best thechniue to separate original wide-type from deamidated potrein is Ion exchange. Ion excjange chromatography separates the protein based on the ions and polariry of the protein/amino acids.

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