Single Molecule Spectroscopy of Protein Folding and Dynamics
We investigate the folding, misfolding, and dynamics of proteins with a close combination of biochemical and spectroscopic methods, particularly single molecule fluorescence.
The folding of proteins, i.e. the formation of a well-defined three-dimensional structure from a linear polypeptide chain, is one of the very fundamental processes of life, intriguing scientists from biology, chemistry and physics. 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. The observation of Förster resonance energy transfer (FRET) between fluorescent dyes coupled to individual protein molecules can be used to quantitatively analyze the structural distributions, their dynamics and the underlying molecular mechanisms.
The following topics are at the center of our current work: