We investigate the folding, misfolding, and dynamics of proteins in a multidisciplinary approach, using a close combination of biophysical and biochemical methods, in particular single molecule fluorescence spectroscopy.

The folding of proteins, i.e. the formation of a well-defined three-dimensional structure from a linear polypeptide chain, is one of the most fundamental processes of life. The failure of proteins to reach their functional structure can lead to the pathological formation of aggregates or amyloid, as found in Alzheimer's disease or Chorea Huntington. Both folding and misfolding are intrinsically heterogeneous processes due to the large number of possible conformations polypeptides can assume. Similarly, many of the functional aspects of proteins are closely linked to their complex interactions and dynamics.

Single molecule spectroscopy, especially in combination with Förster resonance energy transfer (FRET), can be used to resolve such heterogeneity by quantifying structural distributions, their dynamics, and the underlying molecular mechanisms. Toward this goal, we use an integrative approach comprising methods that range from molecular biology to protein chemistry, spectroscopy, instrument/software development, and simulations. Scientists and students from a correspondingly broad range of disciplines closely collaborate in the group.