Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques
The analysis of post-translational modifications by proteomics is regarded as a technically challenging undertaking. While in recent years approaches to examine and quantify protein phosphorylation have greatly improved, the analysis of many protein modifications, such as glycosylation, are still re...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2015-08-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00674/full |
| _version_ | 1828764319622365184 |
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| author | Kristina eFord Wei eZeng Joshua L Heazlewood Joshua L Heazlewood Anthony eBacic |
| author_facet | Kristina eFord Wei eZeng Joshua L Heazlewood Joshua L Heazlewood Anthony eBacic |
| author_sort | Kristina eFord |
| collection | DOAJ |
| description | The analysis of post-translational modifications by proteomics is regarded as a technically challenging undertaking. While in recent years approaches to examine and quantify protein phosphorylation have greatly improved, the analysis of many protein modifications, such as glycosylation, are still regarded as problematic. Limitations in the standard proteomics workflow that can significantly prevent the identification of glycopeptides are the use of suboptimal peptide fragmentation methods. The development of modern tandem mass spectrometers has resulted in the availability of a variety of fragmentation options, many of which are becoming standard features on these instruments. We have used three common fragmentation techniques, namely CID, HCD and ETD, to analyse a plant glycopeptide and highlight how an integrated fragmentation approach can be used to characterize the N-glycan sites of |
| first_indexed | 2024-12-11T02:19:44Z |
| format | Article |
| id | doaj.art-2cba402d699c450f974d18cfdd6f1a41 |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-11T02:19:44Z |
| publishDate | 2015-08-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-2cba402d699c450f974d18cfdd6f1a412022-12-22T01:24:05ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2015-08-01610.3389/fpls.2015.00674147055Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniquesKristina eFord0Wei eZeng1Joshua L Heazlewood2Joshua L Heazlewood3Anthony eBacic4The University of MelbourneThe University of MelbourneThe University of MelbourneLawrence Berkeley National LaboratoryThe University of MelbourneThe analysis of post-translational modifications by proteomics is regarded as a technically challenging undertaking. While in recent years approaches to examine and quantify protein phosphorylation have greatly improved, the analysis of many protein modifications, such as glycosylation, are still regarded as problematic. Limitations in the standard proteomics workflow that can significantly prevent the identification of glycopeptides are the use of suboptimal peptide fragmentation methods. The development of modern tandem mass spectrometers has resulted in the availability of a variety of fragmentation options, many of which are becoming standard features on these instruments. We have used three common fragmentation techniques, namely CID, HCD and ETD, to analyse a plant glycopeptide and highlight how an integrated fragmentation approach can be used to characterize the N-glycan sites ofhttp://journal.frontiersin.org/Journal/10.3389/fpls.2015.00674/fullGlycosylationTandem Mass Spectrometrypost-translational modificationfragmentationElectron-transfer dissociation |
| spellingShingle | Kristina eFord Wei eZeng Joshua L Heazlewood Joshua L Heazlewood Anthony eBacic Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques Frontiers in Plant Science Glycosylation Tandem Mass Spectrometry post-translational modification fragmentation Electron-transfer dissociation |
| title | Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques |
| title_full | Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques |
| title_fullStr | Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques |
| title_full_unstemmed | Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques |
| title_short | Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques |
| title_sort | characterization of protein n glycosylation by tandem mass spectrometry using complementary fragmentation techniques |
| topic | Glycosylation Tandem Mass Spectrometry post-translational modification fragmentation Electron-transfer dissociation |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2015.00674/full |
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