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Klaus Zangger

Walter Becker: Structural characterization of the toxin-coregulated pilus H (TcpH) protein and the characterization of lipopolysaccharides by liquid state NMR.
Sebastian Tassoti: NMR investigations of protein-ligand interactions in living cells

Closed projects
Adam Redzej: Protein Interactions within the Plasmid R1 Relaxosome and their Specific DNA Recognition
Christoph Göbl: Structural studies of membrane-bound toxin-antitoxin systems by NMR spectroscopy
Walter Hohlweg: NMR spectroscopic investigation of toxic bacterial proteins
Gabriel Wagner: Protein structure determination of Vibrio cholerae regulatory proteins
Sergio Pulido: Elucidation of the structure of TcpP protein of V. cholera and determination of its putative molecular interactions using NMR techniques
Krishna Chaitanya Bhattiprolu: Intrinsic disorder in bacterial protein-protein interactions studied by NMR spectroscopy

Further Information
Curriculum Vitae (44 kB)
Publication List (external Link)
Collaborators (60 kB)
Grants (49 kB)


Klaus Zangger
Institute of Chemistry
Karl Franzens Universität Graz
Heinrichstrasse 28
8010 Graz

e-Mail: klaus.zangger@uni-graz.at
phone: +43 316 380 8673
fax: +43 316 380 9840
web: http://www.uni-graz.at/klaus.zangger

Structural NMR studies of bacterial transcription regulation

K. Zangger uses high-resolution NMR (nuclear magnetic resonance) spectroscopy for structure determinations to gain insight into the functioning of biological macromolecules. Main targets have been proteins of bacterial toxin-antitoxin systems and their interactions with DNA. Studies with the antitoxin CcdA and CcdB of the ccd (control of cell death) system of plasmid F and Fst of the par addiction module are exemplary for these interests. Interactions of various parts of CcdA with its corresponding toxin CcdB as well as its cognate DNA allowed insights into its dual role: toxin inhibition and autoregulation. Other work has addressed enzymatic mechanisms of membrane-bound proteins. Recently the group found e.g. that a cation-? interaction in the membrane is essential for the catalytic activity of an ATPase. Another important aspect of K. Zangger’s research is the development of new techniques. His group recently invented an alternative NMR structure determination approach, which is expected to enhance the current size limit of protein studies by NMR spectroscopy. The strategy is based on paramagnetic environment relaxation enhancements (PREs), which provide information about the distance from the surface of individual protein nuclei. A similar technique has been used to monitor protein-protein interactions in the (CcdA)4-DNA complex. More recent work addresses the limited resolution of proton spectra. Homonuclear broadband decoupling allows the separation of many overlapped signals in two- and multidimensional experiments.

Laboratory know-how and infrastructure

The proposed projects will be carried out at the Institute of Chemistry / Organic and Bioorganic Chemistry, University of Graz, Austria. In the Bio-NMR group we have experience with protein NMR, the use of 2D and 3D multinuclear NMR techniques, recombinant protein expression, cell-free protein synthesis, protein handling, pulse sequence development and NMR solution structure determination. At the University of Graz we determined a number of protein structures by NMR (currently 21 entries in the PDB data base, more than any other NMR spectroscopist in Austria). Two structures were featured on the covers of the corresponding journals: the CcdA-DNA structure on the cover of J. Mol. Biol. and the ParD structure (of M. Oberer) on Prot.Sci. Besides the actual structural work we also work on the development of novel techniques, in particular the use of relaxation enhancements in a paramagnetic environment and homonuclear broadband decoupling for higher resolution spectra.The capability of working with larger proteins and protein complexes has been demonstrated by the determination of the CcdA-DNA structure, the re-determination of the maltose-binding protein structure using mainly PREs and the determination of the 35 kDa major allergen Phl p 5.

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