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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
preprintsubmitted on 04.03.2021, 08:13 and posted on 05.03.2021, 04:33 by Maximilian Lebede, Fiammetta di Marco, Wolfgang Esser-Skala, René Hennig, Therese Wohlschlager, Christian G. Huber
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.