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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Pagel, K. Seeberger, P. H. Kolarich, D. Hinneburg, H. Hofmann, J. Struwe, W. B. Altmann, F. Thader, A. Varón Silva, D. |
| Description | Author Affiliation: Hinneburg H ( Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany. daniel.kolarich@mpikg.mpg.de and Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin, 14195 Berlin, Germany. kevin.pagel@fu-berlin.de.); Hofmann J ( Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin, 14195 Berlin, Germany. kevin.pagel@fu-berlin.de and Fritz Haber Institute of the Max Planck Society, 14195 Berlin, Germany.); Struwe WB ( Department of Chemistry, Physical and Theoretical Chemistry Laboratory, University of Oxford, OX1 3QZ, Oxford, UK.); Thader A ( Department of Chemistry, University of Natural Resources and Applied Life Sciences, Vienna, Austria.); Altmann F ( Department of Chemistry, University of Natural Resources and Applied Life Sciences, Vienna, Austria.); Varón Silva D ( Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany. daniel.kolarich@mpikg.mpg.de.); Seeberger PH ( Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany. daniel.kolarich@mpikg.mpg.de and Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin, 14195 Berlin, Germany. kevin.pagel@fu-berlin.de.); Pagel K ( Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin, 14195 Berlin, Germany. kevin.pagel@fu-berlin.de and Fritz Haber Institute of the Max Planck Society, 14195 Berlin, Germany.); Kolarich D ( Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany. daniel.kolarich@mpikg.mpg.de.); |
| Abstract | Differentiating the structure of isobaric glycopeptides represents a major challenge for mass spectrometry-based characterisation techniques. Here we show that the regiochemistry of the most common N-acetylneuraminic acid linkages of N-glycans can be identified in a site-specific manner from individual glycopeptides using ion mobility-mass spectrometry analysis of diagnostic fragment ions. |
| ISSN | 13597345 |
| Journal | Chemical Communications |
| Issue Number | 23 |
| Volume Number | 52 |
| e-ISSN | 1364548X |
| Language | English |
| Publisher | Royal Society of Chemistry |
| Publisher Date | 2016-03-01 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | Subscribed |
| Subject Keyword | Glycopeptides Chemistry Mass Spectrometry Methods N-Acetylneuraminic Acid Journal Article Research Support, Non-U.S. Gov't |
| Content Type | Text |
| Resource Type | Article |
| Subject | Ceramics and Composites Chemistry Surfaces, Coatings and Films Materials Chemistry Metals and Alloys Electronic, Optical and Magnetic Materials Catalysis |
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