Asparagine and glutamine residues in proteins will sometimes be deamidated in as

Question

Asparagine and glutamine residues in proteins will sometimes be deamidated in 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it will result in a mixed population of proteins with the original Asn and Gln residues and proteins in which they have been replaced by Asp and Glu.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?Please explain why?
A) SDS-PAGE
B)Solubility assays(salting out)
C)Gel filtration
D)Ion exchange
The answer A)SDS PAGE is incorrect. Why not?

Explanation / Answer

SDS PAGE is not used for separation of these two proteins because, in SDS PAGE sodium dodecyl sulphate is used which is an anionic detergent that would be denaturing the protein, as a result the proteins will only be separated on the basis of only on the basis of size, hence, the proteins will not be obtained in the native form. As a result, gel permeation or size exclusion or gel filtration will be used where molecule will be separated on the geometry and size of the of the molecule.

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