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It has been observed that Asn and Gln residues in the interior of a protein are

ID: 65496 • Letter: I

Question

It has been observed that Asn and Gln residues in the interior of a protein are delaminated at a much slower rate than Asn and Gln residues on the surface of the protein. Why is this? It has been observed that Asn and Gln residues in the interior of a protein are delaminated at a much slower rate than Asn and Gln residues on the surface of the protein. Why is this? It has been observed that Asn and Gln residues in the interior of a protein are delaminated at a much slower rate than Asn and Gln residues on the surface of the protein. Why is this?

Explanation / Answer

All the deamidation processes require water molecules to go to completion. The more stable and internal protein structures may limit access of water to amide groups and so influence the rates of any deamidation reactions. However surface Asn and Gln are exposed to water molecules which explains the higher rate of protein deamidation. Thus, access to water molecules are the reason of diffeerntial rates of demidation of Asn and Gln.

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