Biomolecular Solid-State-NMR-Spectroscopy
About
We apply solid-state NMR spectroscopy to study protein folding and misfolding in all aspects ranging from intrinsically and partially disordered proteins over oligomeric intermediates to well-ordered amyloid fibrills.
Research Topics
- Solid-State NMR-spectroscopy
- Hyperpolarisation
- DNP-Enhancement
- Protein Folding
- Protein Misfolding
- Amyloid fibrils
The central research focus of our group is the structural characterization of protein folding, misfolding and aggregation (Willbold et al. 2021). Towards this goal, we apply state of the art biomolecular solid-state NMR-spectroscopy (Müller et al. 2013, Beumer et al. 2018).
We exploiting the potential of DNP-enhanced solid state NMR-spectroscopy for investigation of structural ensembles of partly denatured and intrinsically unfolded proteins (Uluca et al. 2018, Viennet et al. 2018, König et al. 2019, Siemons et al. 2019).
We also have investigated details of oligomeric protein assemblies stabilized by N-terminal Prion protein (Rösener et al. 2018, König et al. 2021). We also characterize amyloid fibrils (see, e.g. Heise et al. 2005, Weirich et al. 2016, Gremer et al. 2017).
Dr. Boran Uluca-Yazgi
MSc Nina Becker
MSc Luis Gardon
BSc Christoph Hölbling