Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection.

@article{Mendoza2008ProteinSM,
  title={Protein surface mapping using diethylpyrocarbonate with mass spectrometric detection.},
  author={Vanessa Mendoza and Richard W Vachet},
  journal={Analytical chemistry},
  year={2008},
  volume={80 8},
  pages={2895-904}
}
The reliability and information content of diethylpyrocarbonate (DEPC) as a covalent probe of protein surface structure has been improved when used appropriately with mass spectrometric detection. Using myoglobin, cytochrome c, and beta-2-microglobulin as model protein systems, we demonstrate for the first time that DEPC can modify Ser and Thr residues in addition to His and Tyr residues. This result expands the capability of DEPC as a structural probe because about 25% of the sequence of the… CONTINUE READING