Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.

Protein turnover is a well-controlled process in which polypeptides are constantly being degraded and subsequently replaced with newly synthesized copies. Extraction of composite spectral envelopes from complex LC/MS shotgun proteomics data can be a challenging task, due to the inherent complexity o...

Full description

Saved in:
Bibliographic Details
Main Authors: David Lyon, Maria Angeles Castillejo, Christiana Staudinger, Wolfram Weckwerth, Stefanie Wienkoop, Volker Egelhofer
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:https://doi.org/10.1371/journal.pone.0094692
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1849332488461090816
author David Lyon
Maria Angeles Castillejo
Christiana Staudinger
Wolfram Weckwerth
Stefanie Wienkoop
Volker Egelhofer
author_facet David Lyon
Maria Angeles Castillejo
Christiana Staudinger
Wolfram Weckwerth
Stefanie Wienkoop
Volker Egelhofer
author_sort David Lyon
collection DOAJ
description Protein turnover is a well-controlled process in which polypeptides are constantly being degraded and subsequently replaced with newly synthesized copies. Extraction of composite spectral envelopes from complex LC/MS shotgun proteomics data can be a challenging task, due to the inherent complexity of biological samples. With partial metabolic labeling experiments this complexity increases as a result of the emergence of additional isotopic peaks. Automated spectral extraction and subsequent protein turnover calculations enable the analysis of gigabytes of data within minutes, a prerequisite for systems biology high throughput studies. Here we present a fully automated method for protein turnover calculations from shotgun proteomics data. The approach enables the analysis of complex shotgun LC/MS 15N partial metabolic labeling experiments. Spectral envelopes of 1419 peptides can be extracted within an hour. The method quantifies turnover by calculating the Relative Isotope Abundance (RIA), which is defined as the ratio between the intensity sum of all heavy (15N) to the intensity sum of all light (14N) and heavy peaks. To facilitate this process, we have developed a computer program based on our method, which is freely available to download at http://promex.pph.univie.ac.at/protover.
format Article
id doaj-art-d459744263114b5fa5bd3ac83fce802e
institution Kabale University
issn 1932-6203
language English
publishDate 2014-01-01
publisher Public Library of Science (PLoS)
record_format Article
series PLoS ONE
spelling doaj-art-d459744263114b5fa5bd3ac83fce802e2025-08-20T03:46:11ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0194e9469210.1371/journal.pone.0094692Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.David LyonMaria Angeles CastillejoChristiana StaudingerWolfram WeckwerthStefanie WienkoopVolker EgelhoferProtein turnover is a well-controlled process in which polypeptides are constantly being degraded and subsequently replaced with newly synthesized copies. Extraction of composite spectral envelopes from complex LC/MS shotgun proteomics data can be a challenging task, due to the inherent complexity of biological samples. With partial metabolic labeling experiments this complexity increases as a result of the emergence of additional isotopic peaks. Automated spectral extraction and subsequent protein turnover calculations enable the analysis of gigabytes of data within minutes, a prerequisite for systems biology high throughput studies. Here we present a fully automated method for protein turnover calculations from shotgun proteomics data. The approach enables the analysis of complex shotgun LC/MS 15N partial metabolic labeling experiments. Spectral envelopes of 1419 peptides can be extracted within an hour. The method quantifies turnover by calculating the Relative Isotope Abundance (RIA), which is defined as the ratio between the intensity sum of all heavy (15N) to the intensity sum of all light (14N) and heavy peaks. To facilitate this process, we have developed a computer program based on our method, which is freely available to download at http://promex.pph.univie.ac.at/protover.https://doi.org/10.1371/journal.pone.0094692
spellingShingle David Lyon
Maria Angeles Castillejo
Christiana Staudinger
Wolfram Weckwerth
Stefanie Wienkoop
Volker Egelhofer
Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.
PLoS ONE
title Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.
title_full Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.
title_fullStr Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.
title_full_unstemmed Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.
title_short Automated protein turnover calculations from 15N partial metabolic labeling LC/MS shotgun proteomics data.
title_sort automated protein turnover calculations from 15n partial metabolic labeling lc ms shotgun proteomics data
url https://doi.org/10.1371/journal.pone.0094692
work_keys_str_mv AT davidlyon automatedproteinturnovercalculationsfrom15npartialmetaboliclabelinglcmsshotgunproteomicsdata
AT mariaangelescastillejo automatedproteinturnovercalculationsfrom15npartialmetaboliclabelinglcmsshotgunproteomicsdata
AT christianastaudinger automatedproteinturnovercalculationsfrom15npartialmetaboliclabelinglcmsshotgunproteomicsdata
AT wolframweckwerth automatedproteinturnovercalculationsfrom15npartialmetaboliclabelinglcmsshotgunproteomicsdata
AT stefaniewienkoop automatedproteinturnovercalculationsfrom15npartialmetaboliclabelinglcmsshotgunproteomicsdata
AT volkeregelhofer automatedproteinturnovercalculationsfrom15npartialmetaboliclabelinglcmsshotgunproteomicsdata