Neutron-encoded mass signatures for multi-plexed proteome quantification

We describe a protein quantification method that exploits the subtle mass differences caused by neutron-binding energy variation in stable isotopes. These mass differences are synthetically encoded into amino acids and incorporated into yeast and mouse proteins with metabolic labeling; analysis with...

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Detalles Bibliográficos
Autores principales: Hebert, Alexander S, Merrill, Anna E, Bailey, Derek J, Still, Amelia J, Westphall, Michael S, Streiter, Eric R, Pagliarini, David J, Coon, Joshua J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3612390/
https://www.ncbi.nlm.nih.gov/pubmed/23435260
http://dx.doi.org/10.1038/nmeth.2378
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author Hebert, Alexander S
Merrill, Anna E
Bailey, Derek J
Still, Amelia J
Westphall, Michael S
Streiter, Eric R
Pagliarini, David J
Coon, Joshua J
author_facet Hebert, Alexander S
Merrill, Anna E
Bailey, Derek J
Still, Amelia J
Westphall, Michael S
Streiter, Eric R
Pagliarini, David J
Coon, Joshua J
author_sort Hebert, Alexander S
collection PubMed
description We describe a protein quantification method that exploits the subtle mass differences caused by neutron-binding energy variation in stable isotopes. These mass differences are synthetically encoded into amino acids and incorporated into yeast and mouse proteins with metabolic labeling; analysis with high mass resolution (>100,000) reveals the isotopologue-embedded peptide signals permitting quantification. We conclude neutron encoding will enable high levels of multi-plexing (> 10) with high dynamic range and accuracy.
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spelling pubmed-36123902013-10-01 Neutron-encoded mass signatures for multi-plexed proteome quantification Hebert, Alexander S Merrill, Anna E Bailey, Derek J Still, Amelia J Westphall, Michael S Streiter, Eric R Pagliarini, David J Coon, Joshua J Nat Methods Article We describe a protein quantification method that exploits the subtle mass differences caused by neutron-binding energy variation in stable isotopes. These mass differences are synthetically encoded into amino acids and incorporated into yeast and mouse proteins with metabolic labeling; analysis with high mass resolution (>100,000) reveals the isotopologue-embedded peptide signals permitting quantification. We conclude neutron encoding will enable high levels of multi-plexing (> 10) with high dynamic range and accuracy. 2013-02-24 2013-04 /pmc/articles/PMC3612390/ /pubmed/23435260 http://dx.doi.org/10.1038/nmeth.2378 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Hebert, Alexander S
Merrill, Anna E
Bailey, Derek J
Still, Amelia J
Westphall, Michael S
Streiter, Eric R
Pagliarini, David J
Coon, Joshua J
Neutron-encoded mass signatures for multi-plexed proteome quantification
title Neutron-encoded mass signatures for multi-plexed proteome quantification
title_full Neutron-encoded mass signatures for multi-plexed proteome quantification
title_fullStr Neutron-encoded mass signatures for multi-plexed proteome quantification
title_full_unstemmed Neutron-encoded mass signatures for multi-plexed proteome quantification
title_short Neutron-encoded mass signatures for multi-plexed proteome quantification
title_sort neutron-encoded mass signatures for multi-plexed proteome quantification
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3612390/
https://www.ncbi.nlm.nih.gov/pubmed/23435260
http://dx.doi.org/10.1038/nmeth.2378
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