- Since 10/2014
Rudolf Mößbauer Tenure Track Assistant Professor, Structural Membrane Biochemistry, Technische Universität München
- 07/2010 -09/2014
Postdoctoral Associate, Harvard Medical School, Boston, USA.
Advisor: Prof. Dr. Gerhard Wagner, “Structural and functional studies of membrane proteins in phospholipid nanodiscs”
Postdoctoral Associate, Institute of Organic Chemistry and Biochemistry, Technische Universität München, Germany.
Advisor: Prof. Dr. Horst Kessler, “NMR Spectroscopy of Molecular Chaperones, the p53 Tumorsuppressor Network and Spider Silk Proteins”
Doctoral research, Institute of Organic Chemistry and Biochemistry, Technische Universität München, Germany.
Advisor: Prof. Dr. Horst Kessler „NMR Spectroscopy of Molecular Chaperones, the p53 Tumorsuppressor Network and Spider Silk Proteins“
Oct. 2009: Dr. rer. nat. (grade: summa cum laude)
Intern, Aventis Pharma Germany GmbH, Frankfurt am Main at the division Drug Innovation and Approval, Chemistry.
“Binding studies of compounds to receptors and enzymes by NMR spectroscopy”
Diploma, Institute of Biochemistry, Universität Bayreuth, Germany
Advisor: Prof. Dr. Jochen Balbach, (grade: summa cum laude)
Study of Biochemistry, Universität Bayreuth, Germany
2013 TUM-IAS Hans Fischer Fellowship
2012 Arnold-Sommerfeld Award of the Bavarian Academy of Sciences
2011 Hans-Fischer Award 2011, Chemistry Department, Technische Universität München
2011 Friedrich-Weygand Award 2011 of the Max-Bergmann Kreis
2011 Human Frontier Science Program (HFSP) long-term fellowship
2010 EMBO long-term fellowship
2010 Participation and invited talk at the Nobel-Laureates’ Meeting, Lindau, Germany
Prof. Hagn's research 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.
- Covalently circularized nanodiscs for studying membrane proteins and viral entry. Nature Methods 14 (1), 2016, 49-52
- Cell-free Expressed Bacteriorhodopsin in Different Soluble Membrane Mimetics: Biophysical Properties and NMR Accessibility. Structure 21, 2013, 394-401
- Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins. J. Am. Chem. Soc. 135, 2013, 1919-1925
- A Conformationally Frozen Peptoid Boosts CXCR4 Affinity and Anti-HIV Activity. Angewandte Chemie International Edition 51 (32), 2012, 8110-8113
- A structural view on spider silk proteins and their role in fiber assembly. Journal of Peptide Science 18, 2012, 357-365
- Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53. Nat Struct Mol Biol 18 (10), 2011, 1086-1093
- pH-Dependent Dimerization and Salt-Dependent Stabilization of the N-terminal Domain of Spider Dragline Silk-Implications for Fiber Formation. Angewandte Chemie International Edition 50, 2010, 310-313
- A conserved spider silk domain acts as a molecular switch that controls fibre assembly. Nature 465 (7295), 2010, 239-242
- Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1. Molecular Cell 37, 2010, 344-354
- BclxL Changes Conformation upon Binding to Wild-type but Not Mutant p53 DNA Binding Domain. Journal of Biological Chemistry 285, 2009, 3439-3450