Approximately 60% of human proteins contain lengthy segments lacking stable secondary or tertiary structures, known as intrinsically disordered protein regions (IDRs). These regions have received increasing recognition as key regulators across a spectrum of cellular processes, including mRNA transcription, splicing, protein translation, signaling, and localization to specific biomolecular condensates. Moreover, IDRs are enriched in risk genes that are associated with complex diseases, including neurodevelopmental disorders and cancer (). To execute their functions, IDRs engage in intra- and inter-molecular interactions that are typically transient and highly dynamic, and can adjust their interface depending on the binding partner ().
Our research aims to deepen the understanding of molecular recognition in the dynamic regions of the proteome and transcriptome. By combining computational structural biology, cutting-edge AI models, bioinformatics, and protein NMR spectroscopy, we seek to understand, predict, and design tunable biomolecular interactions crucial for health and disease pathology. Together with our collaborators, we conduct research that spans basic science, drug discovery, interpretation of disease variants, and protein engineering.
Network: In addition to the collaboration within the Otto-Loewi Research Center and MUG, we join forces with researchers from around the world. Our collaborators include (Helmholtz Munich), (SickKids Toronto), (University of Toronto), (TU Wien), (Charles University), and (Durham University).
