Succinimidyl residue formation in hen egg-white lysozyme favors the formation of intermolecular covalent bonds without affecting its tertiary structure.

@article{Desfougres2011SuccinimidylRF,
  title={Succinimidyl residue formation in hen egg-white lysozyme favors the formation of intermolecular covalent bonds without affecting its tertiary structure.},
  author={Yann Desfoug{\`e}res and Julien Jardin and Val{\'e}rie Lechevalier and St{\'e}phane Pezennec and Françoise Nau},
  journal={Biomacromolecules},
  year={2011},
  volume={12 1},
  pages={156-66}
}
Protein chemical degradations occur naturally into living cells as soon as proteins have been synthesized. Among these modifications, deamidation of asparagine or glutamine residues has been extensively studied, whereas the intermediate state, a succinimide derivative, was poorly investigated because of the difficulty of isolating those transient species. We used an indirect method, a limited thermal treatment in the dry state at acidic pH, to produce stable cyclic imide residues in hen… CONTINUE READING
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