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Exploring the Chemical Space of Protein Glycosylation in Noncovalent Protein Complexes: An Expedition Along Different Structural Levels of Human Chorionic Gonadotropin Employing Mass Spectrometry

05 March 2021, Version 1
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

Exploration of a highly glycosylated non-covalent protein comples by mass spectreometry is a challenging task due to isobarisicy of the majority of glycoforms. Integration of data from multiple structural levels (released glycan-glycopeptide-protein subunit-protein complex) by means of computational algorithms permits unraveling the hidden diversity of the human chorionic gonadotropin heterodimer, constituting the base for the study of complex glycosylated protein assemblies.

Keywords

bioinformaitics
biopharmaceuticals
glycoprotein characterization
human chorionic gonaditropin
mass spectrometry

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Now Published

Exploring the Chemical Space of Protein Glycosylation in Noncovalent Protein Complexes: An Expedition along Different Structural Levels of Human Chorionic Gonadotropin by Employing Mass Spectrometry [opens in a new tab]
Maximilian Lebede, Fiammetta Di Marco, Wolfgang Esser-Skala, René Hennig, Therese Wohlschlager, Christian G. Huber journal article
Analytical Chemistry , Volume 93, Issue 30
Online publication date: Jul 21, 2021

Version History

Mar 05, 2021 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv.14153249.v1
D O I: 10.26434/chemrxiv.14153249.v1 [opens in a new tab]

Funding

This work was funded by the Austrian Federal Ministry for Digital and Economic Affairs, the National Foundation of Research, Technology, and Development, a Start-up Grant of the State of Salzburg, as well as the Austrian Science Fund (W1213).

Author’s competing interest statement

Novartis AG / Sandoz GmbH as well as Thermo Fisher Scientific provide financial support for the Christian Doppler Laboratory for Innovative Tools for Biosimilar Characterization. René Hennig is employee of glyXera GmbH, Magdeburg, Germany. The salaries of Wolfgang Esser-Skala and Therese Wohlschlager are fully funded; Christian G. Huber’s salary is partly funded by the Christian Doppler Laboratory for Biosimilar Characterization. The authors declare no other competing financial interest.

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