Helmholtz-Gemeinschaft
Helmholtz Structural Biology > Partners > KIT

Karlsruhe Institute of Technology - KIT

Our research is focused on molecular tools and machineries that are involved in transport across biomembranes. This includes direct bilayer permeabilization by antimicrobial, cell-penetrating and fusogenic peptides, but also specific ion transport by biofilm-inducing peptides and ion channels, as well as highly orchestrated events such as protein translocation and tyrosine-kinase receptor signaling. Solid-state NMR spectroscopy with selective 19F-labels (and/or amino acid type selective 15N-labels) in aligned samples offers the advantage of studying membrane-bound peptides and transmembrane protein segments in a highly sensitive manner under quasi-native conditions, i.e. embedded in any desired lipid composition and at ambient temperature. This way, dynamical properties and structural re-arrangements can be addressed in a biologically relevant environment, and the lipid molecules and morphological changes of the bilayer can be observed at the same time. Our methodological spectrum is rounded off by other biophysical methods, such as circular dichroism (at our ANKA synchrotron-beamline), FRET, DSC, MD simulations (in cooperation), etc., besides the appropriate (micro)biological and functional assays.

 

Publications:

Walther, T.H., A.S. Ulrich Transmembrane helix assembly and the role of salt bridges, Curr. Opinin. Struct. Biol. (2014) 27, 63–68 PubMed

Babii, O., S. Afonin, M. Berditsch, S. Reißer, P.K. Mykhailiuk, V.S. Kubyshkin, T. Steinbrecher, A.S. Ulrich*, I.K. Komarov* Controlling biological activity with light: diarylethene-containing cyclic peptidomimetic, Angew. Chem. Int. Ed. (2014) 53, 3392–3395 PubMed

Walther, T.H., C. Gottselig, S.L. Grage, M. Wolf, A.V. Vargiu, M.J. Klein, S. Vollmer, S. Prock, M. Hartmann, S. Afonin, E. Stockwald, H. Heinzmann, O.V. Nolandt, W. Wenzel, P. Ruggerone, A.S. Ulrich Folding and self-assembly of the TatA translocation pore based on a charge zipper mechanism, Cell (2013) 152, 316–326 PubMed

Tkachenko, A.N., D.S. Radchenko, P.K. Mykhailiuk, S. Afonin, A.S. Ulrich*, I.V. Komarov* Design, synthesis, and application of a trifluoromethylated phenylalanine analogue as a label to study peptides by solid-state 19F NMR spectroscopy, Angew. Chem. Int. Ed., 52, 6504-6507 PubMed

Strandberg, E., J. Zerweck, P. Wadhwani, A.S. Ulrich Synergistic insertion of antimicrobial magainin-family peptides depends on the lipid spontaneous curvature, Biophys. J. (2013) 104, L9–L11 PubMed

Muhle-Goll, C., S. Hoffmann, S. Afonin, S.L. Grage, A.A. Polyanski, D. Windisch, M. Zeitler, J. Bürck, A.S. Ulrich Hydrophobic matching controls the tilt and stability of the dimeric platelet-derived growth factor receptor (PDGFR)β transmembrane segment, J. Biol. Chem. (2012) 287, 26178-26186 PubMed

Wadhwani, P., E. Strandberg, N. Heidenreich, J. Bürck, S. Fanghänel, A.S. Ulrich Self-assembly of flexible  strands into immobile amyloid-like -sheets in membranes as revealed by solid-state 19F-NMR, J. Am. Chem. Soc. (2012) 134: 6512–6515 PubMed

Strandberg E., D. Tiltak, S. Ehni, P. Wadhwani, A.S. Ulrich Lipid shape is a key factor for membrane interactions of amphipathic helical peptides, Biochim. Biophys. Acta - Biomembranes (2012) 1818: 1764–1776 PubMed

Walther T.H., S.L. Grage, N. Roth, A.S. Ulrich Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from B. subtilis resolved by solid-state NMR spectroscopy, J. Am. Chem. Soc. 132, 15945-15956

10. Ieronimo, M., S. Afonin, K. Koch, M. Berditsch, P. Wadhwani, A.S. Ulrich 19F-NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes, J. Am Chem. Soc. (2010) 132: 8822-8824 PubMed

 

 

 

 

30.08.2012

Contact

 

Prof. Dr. Anne Ulrich

Institut für Organische Chemie - Lehrstuhl Biochemie
Fritz-Haber-Weg 6
D-76131 Karlsruhe

 

+49 721 608 43912


Institut für Biologische Grenzflächen (IBG-2)
Postfach 3640
D-76021 Karlsruhe

+49 721 608 23201

www.ibg.kit.edu/

We use cookies to improve your experience on our Website. We need cookies to continuously improve the services, to enable certain features and when embedding services or content of third parties, such as video player. By using our website, you agree to the use of cookies. We use different types of cookies. You can personalize your cookie settings here:

Show detail settings
Please find more information in our privacy statement.

There you may also change your settings later.