The research in our group is focused on the development and application of nuclear magnetic resonance (NMR) spectroscopy to study biomacromolecules. Our focus is to contribute to a molecular understanding of the fundamental mechanism of biomacromolecules. We investigate proteins - soluble proteins and membrane proteins. We investigate RNAs and RNA-protein complexes and unusual DNA structures.

Particular emphasis is on time-resolved NMR experiments; we induce protein, DNA- or RNA-folding by light from compounds that are caged in one (of several) conformations by photolabile protecting groups or natural light-absorbing chromophores. Some of these caged molecules are synthesized in the lab. A different way of inducing biomacromolecular folding is by temperature jump; thus we have developed T-jump probes to do these kinds of experiments.

We also investigate proteins structures to contribute to rational drug discovery and support our mechanistic studies by chemical synthesis.