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Towards the elucidation of the deamidation mechanism of asparaginyl residues in peptides and proteins

Abstract : Deamidation of proteins is a topic of wide interest that has been subject to experimental and theoretical studies. Deamidation is a nonenzymatic and spontaneous process that converts asparagine residues in proteins into aspartic acid. The change in charge leads to time-dependent conformational changes in proteins and has been associated with protein degradation and ageing. In this manuscript, certain mechanistic aspects of this process have been investigated and many insights have been attained on potential mechanisms leading to deamidation. These mechanisms and their energetics have been presented in detail. Another potential fate of asparagine residues, backbone cleavage, has been introduced and compared with the deamidation mechanism. Finally, attempts to understand the effect of neighboring residues on Asn deamidation have been elaborated and several ideas for future work have been outlined.
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https://hal.univ-lorraine.fr/tel-01748278
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Saron Catak. Towards the elucidation of the deamidation mechanism of asparaginyl residues in peptides and proteins. Other. Université Henri Poincaré - Nancy 1, 2007. English. ⟨NNT : 2007NAN10124⟩. ⟨tel-01748278⟩

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