The main goal of our group is the structural characterization of immobilized non-crystalline proteins. In particular we are interested in unfolded and misfolded proteins which play a role in neurodegenerative diseases, such as Aβ, α-synuclein, IAPP and PrP: we look at the fibrillar form (F. Weirich et al. 2016, Plos One 11 20, L. Gremer et al. 2017, Science 358 116., H. Müller, et al. 2014, Prion 8 344.), as well as at the protein in contact with lipid bilayers (T. Viennet et al. 2017, bioRxiv; doi: 10.1101/173724.). Recently we successfully characterized full conformational ensembles of an intrinsically unfolded protein in frozen solution by DNP-enhanced solid-state NMR-spectroscopy (B. Uluca et al. Biophys. J. in press).
Further, we develop methods in solid-state NMR-spectroscopy to further push the limits (T. Viennet et al. 2016, Angew. Chem. Int. Ed. 55 10746).
The focus of our research group is the structural characterization of molecules and molecular complexes which are not accessible by traditional methods for structural characterization such as solution NMR-spectroscopy and X-ray crystallography. In particular for the characterization of membrane proteins in their natural environment (lipid bilayers) as well as misfolded proteins solid-sztate NMR has proven to be extremely useful.
Cross-cutting topic structural biology: solid-state NMR-spectroscopy