I grew up in Gehrden, a small town close to Hannover, Germany. After finishing school we had to do one year of social or military service back then, so I decided to work in an institute for microbiology and hospital hygiene to explore my interest in life sciences. I had a great time learning about infectious diseases, which encouraged me to enrol for a biochemistry degree at my local university. During my degree I started to focus on structural biology as a tool to understand what is going on in a biological system, how to manipulate it, and how to fix it – if it is broken. To do all of that, we can use x-rays generated at particle accelerators to map the position of single atoms in proteins that play a role in diseases. Pretty cool if you ask me. My studies allowed me to travel to New Zealand for research projects and work with big players in the pharmaceutical industry such as Merck. Besides the science, I really enjoy the possibility to travel, meet new people and experience different cultures for my work. So it happens that I find myself now in the beautiful Yorkshire area to complete the next step of my scientific career: a PhD at the University of Leeds, UK.
If I am not in the lab you will find me exploring the lovely countryside or the British pub culture!
university of leeds
start date | 11/09/2017
supervisor | Adrian Goldman
Novel Approaches to Proton Pumping Pyrophosphatases
My PhD project mainly focuses on structural studies of a specific type of enzymes called membrane-bound pyrophosphatases (M-PPases) to better understand how they function. M-PPases contribute the stress resistance of a several bacteria and parasites causing severe diseases, which is one reason why we are interested in them. By solving the structure of these enzymes we can begin to understand their working mechanism and design drugs to interfere with their function and fight their host pathogens that way. We already managed to solve some structures of M-PPases, but there are many unanswered questions remaining. For example: Some M-PPases pump sodium ions (Na+) across biological membranes, some pump protons (H+), and yet others pump both, Na+ and H+. But how do they do that and how do they differentiate between Na+ and H+ ? This is one question I try to answer by solving new M-PPase structures. A structure only provides a single snapshot in time. For a better understanding and a more complete picture we need several snapshots taken at different timepoints to see M-PPases moving as they do their job, just as in a stop motion movie. This is the concept of time-resolved structural studies I am also exploring.
Unfortunately, it is very difficult to obtain protein structures. This is especially true for membrane proteins as we need to extract them out of their natural environment (the membrane) to study them, which often makes them unstable. Of all protein structures solved so far, only about 3% are membrane proteins. Therefore, I also work on the development of new tools that will help us to stabilise membrane proteins by the introduction of mutations or addition of lipids that usually surrounding them in a membrane.
Skills & Expertise
#Construct design and cloning
#Eukaryotic and prokaryotic protein expression
#Protein purification and biochemical characterisation
European Spallation Source (Sweden), 2020 – cancelled due to Covid
Molecular Dimensions (UK), June 2019
University of Hamburg (Germany), February 2019
Imperial College London (UK), January 2018
Workshops & conferences
Astbury Research Retreat, Buxton (UK) | 2017, 2018, 2019
Astbury Conversation, Leeds (UK) | 2018
British Crystallography Association spring meeting, Nottingham (UK) | 2019, 2021
British Crystallography Association winter meeting, London (UK) | 2018
CCP4 study weekend, Nottingham (UK) | 2018, 2019, 2020
High-throughput protein production workshop: Fermentation without tears, Leeds (UK) | 2018
Electron microscopy workshop: Sample preparation and grid screening, Leeds (UK) | 2017
Scientific programming: Introduction to python, Leeds (UK) | 2017
Asymmetry in membrane-bound pyrophosphatases explored by conventional and time-resolved x-ray crystallography. British Crystallography Association spring meeting, UK | 2021
A rational approach to stabilise membrane proteins for structural studies. British Crystallography Association spring meeting, UK | 2019
Jannik has not just been doing research, he has also been involved in science communication activities to engage citizens with science.
Participating to the event “Crystals made of tears: from misery to cheer” at The Devereux pub in central London | July 2019
Blogging about science and PhD life| see all blogposts from Jannik: Portrait, Two weeks in sunny Ireland for the workshop in meso, Last news on solving mPPases structures and Jannik’s view on the MSCA network, Academia vs. industrial secondment
Holding a stall on “The sensational world of G-Protein coupled receptors” at the Astbury conversation organised by the University of Leeds | UK, April 2018