Mass spectral analysis of acetylated peptides: Implications in proteomics ...
Sequence determination of peptides using mass spectrometry plays a crucial role in the bottom-up approaches for the identification of proteins. It is crucially important to minimise false detection and validate sequence of the peptides in order to correctly identify a protein. Chemical modification...
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ftdatacite:10.25384/sage.c.4554038.v1 2024-09-30T14:24:07+00:00 Mass spectral analysis of acetylated peptides: Implications in proteomics ... Chandra, Deepika P Gayathri Mudita Vats R Nagaraj MK Ray MV Jagannadham 2019 https://dx.doi.org/10.25384/sage.c.4554038.v1 https://sage.figshare.com/collections/Mass_spectral_analysis_of_acetylated_peptides_Implications_in_proteomics/4554038/1 unknown Figshare https://dx.doi.org/10.1177/1469066719857564 https://dx.doi.org/10.25384/sage.c.4554038 CC BY 4.0 https://creativecommons.org/licenses/by/4.0 91299 Materials Engineering not elsewhere classified FOS: Materials engineering Collection article 2019 ftdatacite https://doi.org/10.25384/sage.c.4554038.v110.1177/146906671985756410.25384/sage.c.4554038 2024-09-02T09:51:42Z Sequence determination of peptides using mass spectrometry plays a crucial role in the bottom-up approaches for the identification of proteins. It is crucially important to minimise false detection and validate sequence of the peptides in order to correctly identify a protein. Chemical modification of peptides followed by mass spectrometry is an option for improving the spectral quality. In silico -derived tryptic peptides with different N-terminal amino acids were designed from human proteins and synthesized. The effect of acetylation on the fragmentation of peptides was studied. N-terminal acetylation of the tryptic peptides was shown to form b 1 -ions, improve the abundance and occurrence of b-ions. In some cases, the intensity and occurrence of some y-ions also varied. Thus, it is demonstrated that acetylation plays an important role in improving the de novo sequencing efficiency of the peptides. The acetylation method was extended to tryptic peptides generated from the proteome of an Antarctic bacterium ... Article in Journal/Newspaper Antarc* Antarctic DataCite Antarctic |
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91299 Materials Engineering not elsewhere classified FOS: Materials engineering |
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91299 Materials Engineering not elsewhere classified FOS: Materials engineering Chandra, Deepika P Gayathri Mudita Vats R Nagaraj MK Ray MV Jagannadham Mass spectral analysis of acetylated peptides: Implications in proteomics ... |
topic_facet |
91299 Materials Engineering not elsewhere classified FOS: Materials engineering |
description |
Sequence determination of peptides using mass spectrometry plays a crucial role in the bottom-up approaches for the identification of proteins. It is crucially important to minimise false detection and validate sequence of the peptides in order to correctly identify a protein. Chemical modification of peptides followed by mass spectrometry is an option for improving the spectral quality. In silico -derived tryptic peptides with different N-terminal amino acids were designed from human proteins and synthesized. The effect of acetylation on the fragmentation of peptides was studied. N-terminal acetylation of the tryptic peptides was shown to form b 1 -ions, improve the abundance and occurrence of b-ions. In some cases, the intensity and occurrence of some y-ions also varied. Thus, it is demonstrated that acetylation plays an important role in improving the de novo sequencing efficiency of the peptides. The acetylation method was extended to tryptic peptides generated from the proteome of an Antarctic bacterium ... |
format |
Article in Journal/Newspaper |
author |
Chandra, Deepika P Gayathri Mudita Vats R Nagaraj MK Ray MV Jagannadham |
author_facet |
Chandra, Deepika P Gayathri Mudita Vats R Nagaraj MK Ray MV Jagannadham |
author_sort |
Chandra, Deepika |
title |
Mass spectral analysis of acetylated peptides: Implications in proteomics ... |
title_short |
Mass spectral analysis of acetylated peptides: Implications in proteomics ... |
title_full |
Mass spectral analysis of acetylated peptides: Implications in proteomics ... |
title_fullStr |
Mass spectral analysis of acetylated peptides: Implications in proteomics ... |
title_full_unstemmed |
Mass spectral analysis of acetylated peptides: Implications in proteomics ... |
title_sort |
mass spectral analysis of acetylated peptides: implications in proteomics ... |
publisher |
Figshare |
publishDate |
2019 |
url |
https://dx.doi.org/10.25384/sage.c.4554038.v1 https://sage.figshare.com/collections/Mass_spectral_analysis_of_acetylated_peptides_Implications_in_proteomics/4554038/1 |
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Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
https://dx.doi.org/10.1177/1469066719857564 https://dx.doi.org/10.25384/sage.c.4554038 |
op_rights |
CC BY 4.0 https://creativecommons.org/licenses/by/4.0 |
op_doi |
https://doi.org/10.25384/sage.c.4554038.v110.1177/146906671985756410.25384/sage.c.4554038 |
_version_ |
1811639701872836608 |