Prof. Dr. Franz Hagn
Structural Membrane Biochemistry
Academic Career and Research Areas
The research of Professor Hagn (b. 1977) is focused on nuclear magnetic resonance (NMR) spectroscopy of membrane proteins. This protein class is essential for signal transduction and the transfer of proteins and small molecules across the biological membrane barrier. The key to understanding these processes is to study these systems in a native environment provided by a phospholipid bilayer.
Biologically relevant systems of interest are mitochondrial membrane proteins, G-protein coupled receptors (GPCRs) and their associated G-proteins, which are involved in metabolic diseases, neurological disorders and cancer.
Professor Hagn studied biochemistry at the Universities of Bayreuth and Stockholm and moved to TUM to complete a doctorate involving structural and functional studies of molecular chaperones, tumorsuppressor and spider silk proteins. After a short period as a postdoctoral researcher at TUM he joined Harvard Medical School where he worked on the development of native membrane mimics for the structure determination of membrane proteins using NMR. In the fall of 2014 he accepted a Rudolf-Mössbauer assistant professorship of Structural Membrane Biochemistry at the TUM Institute for Advanced Study.
- Arnold-Sommerfeld Award of the Bavarian Academy of Sciences (2012)
- Hans-Fischer Award, TUM (2011)
- Friedrich-Weygand Prize, Max Bergmann Kreis (2011)
- Human Frontier Science Program Long Term Fellowship (2011)
- EMBO Long Term Fellowship (2010)
Hagn F, Etzkorn M, Raschle T, Wagner G: „Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins". J. Am. Chem. Soc. 2013; 135(5): 1919-1925.Abstract
Hagn F, Lagleder S, Retzlaff M, Rohrberg J, Demmer O, Richter K, Buchner J, Kessler H: "Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53". Nat. Struc. Mol. Biol. 2011; 18 (10): 1086-1093.Abstract
Hagn F, Thamm C, Scheibel T, Kessler H: "pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk--implications for fiber formation". Angew. Chem. Intl. Ed. 2011; 50(1): 310-313.Abstract
Hagn F, Eisoldt L, Hardy JG, Vendrely C, Coles M, Scheibel T, Kessler H: "A conserved spider silk domain acts as a molecular switch that controls fibre assembly". Nature. 2010; 465(7295): 239-242.Abstract
Hagn F, Klein C, Demmer O, Marchenko N, Vaseva A, Moll UM, Kessler H: "BclxL changes conformation upon binding to wild-type but not mutant p53 DNA binding domain". J. Biol. Chem. 2009; 285(5): 3439-3459.Abstract