Development of NMR methods for drug development. In particular, site-specifically attached paramagnetic tags (using unnatural amino acids) are employed to identify the binding site, binding orientation and structure of low-molecular weight compounds on protein targets in solution. Currently, this strategy is being established as a tool for fragment-based drug design.
The same tags are deployed to monitor proteins ‘in action’, i.e. as they change their structure during their functional cycle, and to determine the interactions between different proteins.
As a spin-off, pairs of the paramagnetic tags are used to measure accurate distances in proteins by EPR spectroscopy in collaboration with Prof. Daniella Goldfarb (Israel).