Department of Molecular Biophysics (Adam Lange)

Figure: Schematic representation of the type III secretion system. The structure of the needle was determined by our group using a combination of solid-state NMR, electron microscopy, and computer modeling [Loquet et al., Nature 2012, and Acc Chem Res 2013].

   We study protein structure and dynamics using nuclear magnetic resonance in the solid state (solid-state NMR) and a variety of other biophysical methods. In the last decade, solid-state NMR has emerged as a powerful technique in structural biology as it gives access to structural information for systems that are insoluble or do not crystallize easily. Furthermore, the technique allows for the characterization of chemical details (e.g. protonation of side chains) and functionally important protein dynamics. For solid-state NMR investigations, samples are placed in a strong superconducting magnet (external field up to 20 T, i.e. ~400,000 times stronger than the earth’s magnetic field), spun rapidly (up to 100,000 rotations per second; magic-angle spinning), and probed by radio waves. In our group, one focus is on bacterial nanomachines that are involved in infection processes. Furthermore, we characterize membrane proteins in a lipid bilayer environment, for instance non-selective cation channels and rhomboid intra-membrane proteases. Last but not least we continue to develop new solid-state NMR methods.

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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