The reaction converts a neutral amide side chain into a negatively charged carboxylate. The mass changes by roughly one dalton — small enough that it is easy to miss, large enough that a careful mass measurement resolves it.
The charge change is the consequential part. It alters how the molecule behaves in chromatography and, in a folded protein, can disturb the interactions holding the structure together.
Asparagine deamidates far more readily than glutamine. Rate depends strongly on what sits next to it in the sequence — an adjacent glycine, with little steric bulk, allows the intermediate to form much more easily.
This is why two peptides of similar length can have quite different stability profiles. It is a property of the sequence, not of peptides generally.
Dryness, cold and lower pH. The reaction needs water, so lyophilised material is essentially protected; in solution, refrigeration slows it as it slows everything, and neutral-to-slightly-acidic conditions are less favourable than alkaline ones.
This is one of the specific reasons material ships dry and is reconstituted at the point of use rather than in advance.
The reaction converts a neutral amide side chain into a negatively charged carboxylate. The mass changes by roughly one dalton — small enough that it is easy to miss, large enough that a careful mass measurement resolves it.
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