Mass spectrometry- and lysine amidination-based protocol for thermodynamic analysis of protein folding and ligand binding interactions.

@article{Xu2011MassSA,
  title={Mass spectrometry- and lysine amidination-based protocol for thermodynamic analysis of protein folding and ligand binding interactions.},
  author={Ying Bo Xu and I. Falk and Mark Hallen and Michael C Fitzgerald},
  journal={Analytical chemistry},
  year={2011},
  volume={83 9},
  pages={3555-62}
}
Described here is a mass spectrometry-based covalent labeling protocol that utilizes the amine reactive reagent, s-methyl thioacetimidate (SMTA), to study the chemical denaturant-induced equilibrium unfolding/refolding properties of proteins and protein-ligand complexes in solution. The protocol, which involves evaluating the rate at which globally protected amine groups in a protein are modified with SMTA as a function of chemical denaturant concentration, is developed and applied to the… CONTINUE READING

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