Neutron-encoded mass signatures for multiplexed proteome quantification

Alexander S. Hebert, Anna E. Merrill, Derek J. Bailey, Amelia J. Still, Michael S. Westphall, Eric R. Strieter, David J. Pagliarini, Joshua J. Coon

Research output: Contribution to journalArticle

126 Scopus citations


We describe a protein quantification method called neutron encoding that exploits the subtle mass differences caused by nuclear binding energy variation in stable isotopes. These mass differences are synthetically encoded into amino acids and incorporated into yeast and mouse proteins via metabolic labeling. Mass spectrometry analysis with high mass resolution (>200,000) reveals the isotopologue-embedded peptide signals, permitting quantification. Neutron encoding will enable highly multiplexed proteome analysis with excellent dynamic range and accuracy.

Original languageEnglish
Pages (from-to)332-334
Number of pages3
JournalNature Methods
Issue number4
StatePublished - Apr 2013
Externally publishedYes

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    Hebert, A. S., Merrill, A. E., Bailey, D. J., Still, A. J., Westphall, M. S., Strieter, E. R., Pagliarini, D. J., & Coon, J. J. (2013). Neutron-encoded mass signatures for multiplexed proteome quantification. Nature Methods, 10(4), 332-334.