We investigate the structure, folding, and dynamics of proteins with single-molecule spectroscopy, especially single-molecule Förster resonance energy transfer (FRET). These methods are ideal for studying dynamic systems, even under conditions of pronounced conformational heterogeneity, e.g. for proteins in non-native or disordered states. Single-molecule spectroscopy thus provides an opportunity for probing conformational changes in biological macromolecules, intrinsically disordered proteins (IDPs), the interactions of proteins with molecular chaperones, protein misfolding, and even proteins inside live cells over a wide range of timescales.

Addressing these questions requires a broad spectrum of complementary methods and a multidisciplinary team of scientists from physics, chemistry, and biology that closely collaborate within the group. We use an integrative approach with techniques ranging from molecular biology and protein chemistry to a wide range of biophysical methods and single molecule spectroscopies, instrument and software development, and simulations. The projects require the continuous development and adaptation of single-molecule fluorescence spectroscopy techniques and analysis methods to maximize the information available from the measurements. A key goal of our work is to reach a mechanistic understanding of the systems we study that is based on a quantitative physical description.