Single-molecule spectroscopy of protein folding, disorder, and dynamics
We investigate the structure and dynamics of proteins with optical single-molecule spectroscopy. In particular, we focus on systems with pronounced conformational heterogeneity that is difficult to resolve with other techniques. Examples are intrinsically disordered proteins (IDPs), proteins interacting with molecular chaperones, protein misfolding, or the behavior of proteins inside live cells. A key goal of our work is to reach mechanistic understanding based on quantitative physical models.
Addressing these questions requires a broad spectrum of complementary methods, and thus a multidisciplinary team of scientists from physics, chemistry, and biology who closely collaborate within the group. We use an integrative approach ranging from molecular biology and protein chemistry to a wide range of biophysical methods, single-molecule spectroscopies, and simulations. An important aspect of our research is the continuous development and adaptation of advanced single-molecule techniques and analysis methods for probing biological macromolecules over a wide range of conditions and timescales.