A rather unfamiliar but crucial post-translational modification lies at the center of my research: ADP-ribosylation. Originating from NAD+, ADP-ribosylation comes in several different forms and is attached to target molecules of all kinds, depending on the enzyme catalyzing the reaction. While my master's work centered on bacterial ADP-ribosylating toxins, my current interest lies in their human counterparts - the PARP family. These proteins' functions are as wide-ranging as their structural diversity. Somehow, they must be active in the right place and at the right time to maintain cellular housekeeping and to assist in stress-related responses. Precisely how their activity is regulated is what I am trying to assess, specifically in the case of PARP15 and PARP16. To do so, I use recombinantly produced protein from E.coli and many biochemical and biophysical methods, ranging from specialized PARP-specific assays to more general methods such as fluorescence polarization, circular dichroism, (Hydrogen-Deuterium-Exchange) mass spectrometry, mass photometry, or microscale thermophoresis, to name a few.

I am always open to interdisciplinary collaborations, especially in cell biology.

Research Group

Herwig Schüler

Colleagues

Constantinos Chatzicharalampous

KEMA03 - Biokemi, grundkurs (teaching assistant)

MOBA02 - Biochemistry of the Cell (teaching assistant)