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Data on the peptide mapping and MS identification for phosphorylated peptide

This article contains peptides mapping, mass spectrometry and processed data related to the research “Identification and quantification of the phosphorylated ovalbumin by high resolution mass spectrometry under dry-heating treatment” [1]. Fourier transform ion cyclotron mass spectrometry (FTICR MS)...

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Detalles Bibliográficos
Autores principales: Wang, Hui, Tu, Zong-cai, Liu, Guang-xian, Zhang, Lu, Chen, Yuan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4885016/
https://www.ncbi.nlm.nih.gov/pubmed/27274527
http://dx.doi.org/10.1016/j.dib.2016.05.009
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author Wang, Hui
Tu, Zong-cai
Liu, Guang-xian
Zhang, Lu
Chen, Yuan
author_facet Wang, Hui
Tu, Zong-cai
Liu, Guang-xian
Zhang, Lu
Chen, Yuan
author_sort Wang, Hui
collection PubMed
description This article contains peptides mapping, mass spectrometry and processed data related to the research “Identification and quantification of the phosphorylated ovalbumin by high resolution mass spectrometry under dry-heating treatment” [1]. Fourier transform ion cyclotron mass spectrometry (FTICR MS) was used to investigate the specific phosphorylation sites and the degree of phosphorylation (DSP) at each site. Specifically, phosphorylated peptides were monitored through mass shift on the FTICR MS spectrum. DSP was evaluated through the relative abundance levels of the FTICR MS spectrometry. From these data, the calculation method of DSP was exemplified.
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spelling pubmed-48850162016-06-07 Data on the peptide mapping and MS identification for phosphorylated peptide Wang, Hui Tu, Zong-cai Liu, Guang-xian Zhang, Lu Chen, Yuan Data Brief Data Article This article contains peptides mapping, mass spectrometry and processed data related to the research “Identification and quantification of the phosphorylated ovalbumin by high resolution mass spectrometry under dry-heating treatment” [1]. Fourier transform ion cyclotron mass spectrometry (FTICR MS) was used to investigate the specific phosphorylation sites and the degree of phosphorylation (DSP) at each site. Specifically, phosphorylated peptides were monitored through mass shift on the FTICR MS spectrum. DSP was evaluated through the relative abundance levels of the FTICR MS spectrometry. From these data, the calculation method of DSP was exemplified. Elsevier 2016-05-12 /pmc/articles/PMC4885016/ /pubmed/27274527 http://dx.doi.org/10.1016/j.dib.2016.05.009 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Wang, Hui
Tu, Zong-cai
Liu, Guang-xian
Zhang, Lu
Chen, Yuan
Data on the peptide mapping and MS identification for phosphorylated peptide
title Data on the peptide mapping and MS identification for phosphorylated peptide
title_full Data on the peptide mapping and MS identification for phosphorylated peptide
title_fullStr Data on the peptide mapping and MS identification for phosphorylated peptide
title_full_unstemmed Data on the peptide mapping and MS identification for phosphorylated peptide
title_short Data on the peptide mapping and MS identification for phosphorylated peptide
title_sort data on the peptide mapping and ms identification for phosphorylated peptide
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4885016/
https://www.ncbi.nlm.nih.gov/pubmed/27274527
http://dx.doi.org/10.1016/j.dib.2016.05.009
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