Scientific Coordinator: Adam Lange

Molecular pharmacology requires structural information on all length and time scales. Contributions of NMR spectroscopy typically include high-resolution structural investigations on target systems, studies of their interactions with drug-like molecules, and imaging at the level of organisms. As a spectroscopic technique, NMR serves ‘metabolomics’ studies and investigations on the effects of dynamics in biological processes. Future pharmacology-oriented structural studies are expected to provide information on how super-molecular arrangements assemble and disassemble within the cell, and how these processes are controlled in vivo by protein expression, degradation, post-translational modification as well as through the application of small-molecule or protein-based drugs. The dynamic nature of these phenomena demands the application of NMR, exploiting its triple capabilities of structure determination, spectroscopy, and imaging. Integrating these and other biophysical data with molecular modelling and cheminformatics methods is essential for deriving a comprehensive picture of pharmacological processes as a basis for ligand design.


Department Molecular Biophysics (Adam Lange)

We use solid-state NMR spectroscopy and a variety of other biophysical methods to study protein structure and dynamics. The systems of interest comprise membrane proteins in the context of a native-like lipid bilayer environment and supramolecular assemblies such as type three secretion needles or cytoskeletal filaments.


Department NMR-supported Structural Biology (Hartmut Oschkinat)

The Oschkinat lab focuses on the structural characterisation of protein-protein interactions responsible for the reception and transduction of signals in biological systems. We are interested in protein domains which recognise specific peptides and in membrane integrated receptors and receptor-ligand complexes.


Structural Interactomics (Fan Liu)

Our group is interested in developing and applying tools to characterize the complexity of protein interactions within the cell. Using state-of-the-art mass spectrometric technologies, in particular cross-linking mass spectrometry (XL-MS), we aim to chart the protein interactomes of complex biological systems. This allows us to visualize how proteins are spatially organized and dynamically regulated in vivo, which is fundamental to the understanding of the molecular physiology of the cell.

Junior Research Group: Integrated Structural Dynamics (Sigrid Milles)

Protein dynamics are critically important in many biological processes and intrinsically disordered proteins, i.e. proteins without stable secondary and tertiary structure, are an extreme example for protein dynamics. Our group is studying those highly flexible protein systems using integrated single molecule fluorescence and nuclear magnetic resonance (NMR) spectroscopy techniques that we are also developing.  We are particularly interested in the process of clathrin mediated endocytosis, which exploits a high number of intrinsically disordered proteins, coordinated in an intricate interaction network, for the initiation for this important cellular uptake pathway.

Junior Research Group: Structure and mechanism of microbiome-driven diseases (Daniel Roderer)

We are interested in the molecular mechanism of host-microbiome interactions in the human intestinal system, which play important roles in onset and progression of diseases. We therefore apply Cryo-EM to solve the structures of protein complexes that facilitate epithelial adhesion of bacteria. In addition, we apply genomic and biochemical screening methods to identify yet undescribed microbial proteins that are involved in carcinogenesis.


Junior Research Group: Molecular Imaging (Leif Schröder)

Our group works on the development of magnetic resonance detection techniques for novel targeted contrast agents.


Core Facility: NMR (Peter Schmieder/ Hartmut Oschkinat)

The NMR facility maintains the NMR spectrometers of the FMP and supports researchers from inside and outside the FMP in using state-of-the-art NMR spectroscopy, either solid state or solution state and either in collaborations or by providing a walk-on service for routine NMR spectroscopy.

Core Facility: Mass Spectrometry (Fan Liu)

The mass spectrometry facility hosts state-of-the-art infrastructure for protein characterization. This includes high-end MS technologies for protein identification, quantification, post-translational modification and interaction analysis.


Computational Chemistry / Drug Design  (Ronald Kühne)

We are concerned with the study of protein-protein, protein-ligand interactions, and ligand design by computational algorithms. Our work involves a wide range of molecular modeling technologies, bioinformatics tools, and expertise in NMR structure calculations.


Structural Bioinformatics and Protein Design (Gerd Krause)
Please note: the research group terminated work at the end of 2020, but Jonas Protze and Gerd Krause continue working on completing their common DFG funded project  ‘Searching for transport proteins for TRIAC acting as T3 /TH substitutes’. Here you can read more about it.

We focus on the analysis of proteins by structural bioinformatics combined with experimental functional studies of changed sequence(s) to reveal sequence- and structure-function relationships of proteins. Our aim is the rational discovery of molecular mechanisms and sites for protein-protein interactions and protein-ligand interaction.


Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10
13125 Berlin, Germany
+4930 94793 - 100 
+4930 94793 - 109 (Fax)

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