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Neutron-encoded mass signatures for multiplexed proteome quantification
Journal article   Open access   Peer reviewed

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 and Joshua J Coon
Nature methods, Vol.10(4), pp.332-334
04/2013
DOI: 10.1038/nmeth.2378
PMCID: PMC3612390
PMID: 23435260
url
https://www.ncbi.nlm.nih.gov/pmc/articles/3612390View
Open Access

Abstract

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.
Deuterium Gene Expression Regulation, Fungal Saccharomyces cerevisiae - genetics Carbon Isotopes Neutrons Saccharomyces cerevisiae Proteins - genetics Nitrogen Isotopes Protein Sorting Signals Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism Proteomics - methods Chromatography, Liquid - methods Tandem Mass Spectrometry - methods Saccharomyces cerevisiae Proteins - chemistry

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