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| Research Group Lange |
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Solid-state NMR
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In the last decade, magnetic resonance in the solid state (solid-state NMR) has emerged as a powerful technique in structural biology as it gives access to structural information for systems which are insoluble or do not crystallize easily. For instance, solid-state NMR opens new ways to study membrane proteins in their natural lipid environment, or insoluble disease-associated protein aggregates. Moreover, functional filamentous assemblies such as the needle of the type three secretion system – composed of multiple copies of a single small protein – can be readily studied.
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In terms of membrane proteins, our main interest lies on the voltage-dependent anion channel (VDAC) that is located in the mitochondrial outer membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites [
 Lange et al., Nature, 2006;
Schneider et al., Angew. Chem. 2010].
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Another focus of our research is the structural characterization of amyloid fibrils formed by the proteins tau or α-synuclein that are involved in neurodegenerative diseases [ Wasmer, Lange, Van Melckebeke et al., Science 2008;
Loquet et al., JACS 2010].
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Furthermore, we have recently started to structurally characterize the needle of the S. typhimurium type three secretion system, a complex nanomachine involved in bacterial infection [Poyraz, Schmidt, Seidel et al., Nat. Struct. Mol. Biol. 2010].
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In terms of solid-state NMR method development, the focus is on new experiments using ultra-fast magic-angle spinning and low radio-frequency deposition with the goal to further improve resolution and sensitivity of biological solid-state NMR spectroscopy. Additionally, we exploit sparse isotope-labeling schemes that enhance spectral resolution and facilitate resonance assignment and detection of long-range distance restraints [ Vijayan et al., ChemPhysChem 2009;
Demers et al., J. Magn. Reson. 2010;
Loquet et al., JACS 2011].
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Finally, we are also interested in the application of solid-state NMR to inorganic chemistry and polymer science [ Sen et al., Angew. Chem. 2011;
Tatic et al., Angew. Chem. 2011].
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© 2011, Max Planck Institute for Biophysical Chemistry, Göttingen |
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