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The group develops novel tools for the application of NMR spectroscopy to the study of biological macromolecules (proteins and DNA). Emphasis is placed on the study of protein-protein, protein-DNA and protein-ligand interactions, with applications for drug development in the pharmaceutical industries in mind. In particular, NMR is used to determine the three-dimensional (3D) structures of protein domains and protein-ligand complexes. This research is supported by 800 and 600 MHz NMR spectrometers equipped with a cryoprobe.
Gottfried Otting received his Diploma of Chemistry from the University of Freiburg and completed his PhD at ETH-Zürich.
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The cell-free expression system available in-house was enhanced by a protocol that allows the expression of proteins from linear PCR-amplified DNA.
A generic protocol was developed that allows site-specific tagging of proteins with a lanthanide-binding peptide or organic molecule.
The 3D structure of the monomeric C-terminal domain of the E. coli primase DNA-G was determined by NMR spectroscopy.
The 3D structure of the 30 kDa complex formed between the E. coli proteins epsilon and theta with the small ligand thymidine was determined.
More about Structure Determination of a Protein-Ligand Complex Using Paramagnetic NMR