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Solid-State NMR-Spectroscopy and DNP-enhancement

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).
Another aspect of our research is the exploration of the hyperpolarization technique DNP to probe the mobility of surface-bound functional groups (Park et al. 2020).

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