My lab aims at understanding how proteins fold, interact and associate in larger structures in their native environments. We interrogate proteins by two approaches that we developed in our lab. Both base on imaginative computational interrogation of mass spectrometric data that we obtain ourselves using advanced mass spectrometers.
We are one of the key pioneering labs staging the transition of cross-linking/mass spectrometry into a powerful and useful addition to the structural biology toolbox. These advances included developing algorithms, software, protocols and mass spectrometric acquisition details. We thoroughly tested and then exploited these tools in numerous biological applications in our own lab and in collaboration with world-leading scientists in their respective disciplines. These efforts included the first analysis of a large multi-protein complex using cross-linking/mass spectrometry (RNA Pol II-TFIIF). We also spearheaded further developments in quantitative cross-linking/mass spectrometry using stable isotopes.
In a second research line, we propose a fundamentally new view on analysing protein localisation and possibly on localisation itself.
Trying to establish a definitive list of proteins that associate with mitotic chromosomes in vertebrates we realised shortcomings in standard concepts of organellar proteomics (that the composition of an organelle can be defined through biochemical purification). We developed a different approach by analysing the composition of mitotic chromosome preps obtained in multiple different ways and integrating this by machine learning. We expanded this conceptually in several ways and proposed a view of interphase chromatin that helped define replicating chromatin.