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.


Junior Research Group: Molecular Imaging (Leif Schröder)

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



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)

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.




Protein Engineering (Christian Freund)

We are interested in the understanding and manipulation of molecular interactions that govern the assembly of protein complexes. The focus is on scaffolding proteins that mediate non-covalent interactions in immune cells and other eukaryotic cells.

Please note that Christian Freund was appointed Professor at the Freie Universität Berlin in 2011.

Solid-State NMR (Bernd Reif)

Our group is interested in biomolecular systems that are situated at the interface between solution and solid. In this area, membrane proteins and amyloidogenic peptides and proteins are the most interesting "target molecules".

Please note that Bernd Reif was appointed Professor at the Technische Universität München in 2010.

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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