Biomolecular Solid-State-NMR-Spectroscopy


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


Prof. Henrike Heise


Building 05.8v / Room 3025

+49 2461/61-4658 1934


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

Projekts and Cooperations
Selected Publications

Last Modified: 22.01.2023