Structural dynamics in biomolecular interactions
Cellular processes are driven by biomolecular interactions, and their regulation often hinges on dynamics rather than static structures. Biomolecules continuously sample thermodynamic states, and these transitions critically shape recognition and function. We use nuclear magnetic resonance (NMR) spectroscopy to characterize these dynamics at atomic resolution across diverse interaction networks involving proteins, nucleic acids, lipids, carbohydrates, and small molecules. Our focus spans key biological contexts, including epigenetic inheritance and antibiotic action. By elucidating how biomolecules undergo disorder-to-order transitions, we aim to uncover general principles linking dynamics to function.
NMR as a window into conformational dynamics of biomolecules
We target two fundamental aspects of biomolecular dynamics. First, we map conformational changes—ranging from large-scale domain movements to local side-chain rotations and loop flexibility—capturing how binding and recognition reshape structure. Second, we probe how chemical modifications regulate these dynamics by altering charge distribution, protonation states, hydrogen-bonding networks, and molecular interactions. Examples include nucleotide base modifications in nucleic acids or post-translational modifications like serine phosphorylation in proteins. Together, these studies reveal how both structural flexibility and chemical fine-tuning act in concert to control biomolecular interactions, advancing our understanding of molecular regulation and providing new avenues for therapeutic strategies.
Collaborations
We are a highly collaborative group and are always looking for new research cooperation. Please contact Daniel Friedrich (daniel.friedrich[at]uni-koeln.de) if you want to work with us on understanding biomolecular function by NMR.
We are currently working with the groups of Bart Thomma (Department of Biology, University of Cologne) and Alvaro Mallagaray (Institute of Chemistry and Metabolomics, University of Lübeck) on protein-cell wall interactions, with the lab of Ines Neundorf (Department of Chemistry and Biochemistry, University of Cologne) on structural characterization of antimicrobial peptides and with the group of Uli Baumann (Department of Chemistry and Biochemistry, University of Cologne) on analyzing protein-protein interactions. We are also associated with the Collaborative Research Center (CRC) 1211 of the Deutsche Forschungsgemeinschaft.