Atomic structure and conduction mechanism of viral proton channels in liposomes studied by solid-state NMR

Principal Investigator: Prof. Dr. Adam Lange (FMP)

We aim towards a comprehensive understanding of the conduction mechanism of viral proton channels from the West Nile and Dengue viruses. For this purpose we will produce the channels in our lab recombinantly and subject these to solid-state NMR spectroscopy that allows addressing their atomic structures and functionally relevant protein dynamics in liposomes under physiological conditions. In addition, we will focus on the protonation states of functionally important residues and the interaction of the pore-lining residues with water molecules.

Publications

2021-2024

Mohr, S., Aldakul, Y. K., Sun, H., Sawczyc, H., and Lange, A. (2023). Mechanistic Studies of Membrane Proteins Using Integrated Solid-state NMR and Computational Approaches. In Integrated Structural Biology, ed. T. Polenova, C. M. Quinn, and A. M. Gronenborn, Royal Society of Chemistry, vol. 30, ch. 9: pp. 268-300. doi: 10.1039/bk9781837670154-00268.

Paschke, R.R., Mohr, S., Lange, S., Lange, A. and Kozuch, J. (2023). In Situ Spectroscopic Detection of Large-Scale Reorientations of Transmembrane Helices During Influenza A M2 Channel Opening. Angew Chem Int Ed Engl, 62, 47: e202309069. doi: 10.1002/anie.202309069.