Journal article

Characterization of protein N-glycosylation by tandem mass spectrometry using complementary fragmentation techniques

Kristina L Ford, We Zeng, Joshua L Heazlewood, Antony Bacic

Frontiers in Plant Science | FRONTIERS MEDIA SA | Published : 2015

Abstract

The analysis of post-translational modifications (PTMs) 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, such as use of suboptimal peptide fragmentation methods, can significantly prevent the identification of glycopeptides. The current generation of tandem mass spectrometers has made available a variety of fragmentation options, many of which are becoming standard features on these instruments. We have used three common f..

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Grants

Awarded by Australian Research Council (ARC)


Awarded by U. S. Department of Energy, Office of Science, Office of Biological, and Environmental Research


Awarded by ARC Future Fellowship


Funding Acknowledgements

The interpretation of ETD spectra was conducted with the assistance of Ms. Yin Ying Ho (The University of Melbourne). This work was funded by grants from the Australian Research Council (ARC) to the ARC Centre of Excellence in Plant Cell Walls [CE110001007] and the U. S. Department of Energy, Office of Science, Office of Biological, and Environmental Research, through contract DE-AC02-05CH11231 between Lawrence Berkeley National Laboratory and the U.S. Department of Energy. JH is supported by an ARC Future Fellowship [FT130101165]. The MS spectra were acquired at the Mass Spectrometry and Proteomics Facility (MSPF), Bio21 Institute, The University of Melbourne with the help of Dr. Ching-Seng Ang.