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More than 50% of the proteins encoded by the human genome are predicted to
be glycosylated. Glycoproteins are proteins that are modified with specific
sugar structures during and after protein synthesis. Though these sugar
structures differ in their final furnishing dependant of the organism, the
initial biosynthetic steps are highly conserved within all eukaryotic species
known to mankind so far. What do yeasts and your brain cells have in common?
The initial steps of protein glycosylation! :-)
The fact that these initial mechanisms are essentially unchanged in all
eukaryotic beings points is one indicator pointing towards the importance of
protein glycosylation. The last steps of glycosylation differ significantly
between the organisms and these steps appear to be crucial for the fine tuning
of the biological roles of glycoproteins within their particular organism.
A major focus of the Glycoproteomics group here at the Biomolecular Systems
Department is studying glycoproteins and their biological role. Glycoproteins
are known to be crucial for cell-cell interactions, in host-pathogen
interactions and have also been shown to crucially mediate the fusion of the
sperm and egg cell, to just name a few examples.
Another major focus is the development of new methods using mass
spectrometry (ESI, MALDI) which allow us new insights and better understanding
of these interesting biomolecules.
The group is always looking for interested and motivated master and PhD
students.
Structure of an IgM Cryoglobulin (pdb database
structureId=2AGJ)

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