Biomolecular NMR Spectroscopy
We work with structural biology of proteins and their complexes with other molecules (proteins, DNA, drugs). Using NMR spectroscopy, we study the proteins in aqueous solution, i.e. under near-physiological conditions. In particular we work with the development of new methods for studying complexes of greater molecular weight and applications in drug discovery.
Check out the project descriptions on the right and our recent publications for more information about current projects!
Chemical shift changes due to pseudocontact shifts
in a protein with Y3+
(red) or Er3+
Pseudocontact shifts are easy to measure.
3D model of a protein determined by pseudocontact shifts (PCS),
using 4 different lanthanide tagging sites. PCSs reach over long
Lanthanide ions are strong paramagnets. Site-specific attachment of a paramagnetic lanthanide to a protein generates large chemical shift changes in NMR spectra, which encode long-range structural restraints. The method provides structural information on protein-protein, protein-DNA and protein-ligand complexes with record-breaking speed and accuracy. Find out more here.
Cell-free protein synthesis and unnatural amino acids
Making proteins from cDNA can be done in a day using cell-free protein synthesis. The technique is particularly suited for making proteins with selectively stable-isotope labelled proteins for NMR analysis. In addition, it enables efficient site-specific and selective incorporation of different unnatural amino acids. The group is a world-leader in the technology. Find out more here.
The vast majority of drugs are compounds that bind very tightly to a target protein. Knowing how they bind (site, structure, orientation) is key to finding improved molecules in a rational approach. We characterize the 3D structures of target proteins and their complexes with ligands by NMR spectroscopy. Find out more here.