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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.
Proteins are long-chain macromolecules that are usually folded three-dimensionally into a complex architecture. To understand the function of a protein, it is helpful to know its structure. Researchers usually study proteins in soluble or crystalline form. However, many proteins cannot be easily investigated in this way, for instance membrane proteins in a lipid bilayer. For this reason we also use solid-state nuclear magnetic resonance spectroscopy (solid-state NMR) to analyze the structure and dynamics of proteins. This technique allows us to study insoluble and non-crystalline proteins and in addition to protein structure also to investigate chemical details, interaction with water and lipid molecules, and functionally relevant protein dynamics. The latter aspect is important because proteins are not rigid structures with a fixed architecture, but have moving parts similar to machines. To conduct solid-state NMR investigations, we place samples in a strong superconducting magnet (external field up to 20 T, i.e. ~400,000 times stronger than the earth’s magnetic field), rotate them rapidly (up to 100,000 revolutions per second; magic-angle spinning) and investigate them spectroscopically using radio waves. Important applications of our work are the analysis of membrane proteins in their natural lipid environment and the 3D structure determination of cellular molecular machines.
PDB ID:6YQ5
M. Zinke, K. A. A. Sachowsky, C. Öster, S. Zinn-Justin, R. Ravelli, G. F. Schröder, M. Habeck, A. Lange, Architecture of the flexible tail tube of bacteriophage SPP1, Nature Communications, 11 (2020), 5759.
PDB ID:2LPZ 2MEX
A. Loquet, B. Habenstein, V. Chevelkov, S. K. Vasa, K. Giller, S. Becker, and A. Lange, Atomic structure and handedness of the building block of a biological assembly, Journal of the American Chemical Society, 135 (2013), pp. 19135-19138.
A. Loquet, N. G. Sgourakis, R. Gupta, K. Giller, D. Riedel, C. Goosmann, C. Griesinger, M. Kolbe, D. Baker, S. Becker, and A. Lange, Atomic model of the type III secretion system needle, Natu ...
PDB ID:2MME
J.-P. Demers, B. Habenstein, A. Loquet, S. K. Vasa, K. Giller, S. Becker, D. Baker, A. Lange* and N. G. Sgourakis*, High-resolution structure of the Shigella type-III secretion needle determined by solid-state NMR and cryo-electron microscopy, Nature Communications, 5 (2014), 4976.
PDB ID:2N3D
C. Shi, P. Fricke, L. Lin, V. Chevelkov, M. Wegstroth, K. Giller, S. Becker, M. Thanbichler, and A. Lange, Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR, Science Advances, 1 (2015), e1501087.
S. Vasa, L. Lin, C. Shi, B. Habenstein, D. Riedel, J. Kühn, M. Thanbichler, and A. Lange, β-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR, Proceedings of the National Academy o ...
PDB ID:2N7H
B. Habenstein, A. Loquet, S. Hwang, K. Giller, S. K. Vasa, S. Becker, M. Habeck, and A. Lange, Hybrid structure of the type 1 pilus of uropathogenic Escherichia coli, Angewandte Chemie-International Edition, 54 (2015), pp. 11691-11695.
People
Currently, we have open positions for highly motivated PhD and Master’s students and post-doctoral fellows. Candidates with a background in biochemistry, biophysics or related subjects and a strong interest in spectroscopy and/or structural biology.
The Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP) is part of the Forschungsverbund Berlin e.V. (FVB), which legally represents seven non-university research institutes - members of the Leibniz Association - in Berlin.
Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP)
Campus Berlin-Buch
Robert-Roessle-Str. 10,
13125 Berlin, Germany
