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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)...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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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. |
format | Online Article Text |
id | pubmed-4885016 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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