Prof. Dr. Christian Freund

Prof. Dr. Christian Freund

Freie Universität Berlin
Institute for Chemistry & Biochemistry
Thielallee 63
14195 Berlin
Phone: +49 (30) 838 51189
Fax: +49 (30) 838 56413

Research Area

Molecular Cell Biology, Biochemistry, Biophysics

Position and Status

Professor of Protein Biochemistry (W2)

Scholarships and awards

2009    Joint grant recipient and winner of the “Innovationswettbewerb Medizintechnik” of the German Ministry of Education and Research
1999    Biofuture award of the German Ministry of Education and Research
1997    Post-doctoral scholarship of the Swiss National Funds

Academic Education

1986 - 1989   Chemistry, Ludwig-Maximilians-Universität München
1983 - 1986   Chemistry, Heinrich-Heine-Universität Düsseldorf


University Degrees

2005   Venia legendi: Biochemistry, Freie Universität Berlin; 2005
1994   PhD at Max-Planck-Institute of Biochemistry/LMU München, AG NMR (Holak), Department of Structural Biology (Huber)



2011 -            Full professor of Biochemistry (W2), FU Berlin
2000 - 2011   Independent research group leader, Leibniz-Institute of Molecular Pharmacology, Berlin
1997 - 2000   Joint appointment post-doctoral fellow at Harvard Medical School/Dana-Farber-Cancer Institute in Boston with Prof. Gerhard Wagner and Prof. E. Reinherz (Scholarship by the Swiss National Funds)
1994 - 1997   Postdoctoral fellow in the group of Prof. Dr. A. Plückthun, Biochemical Institute of the University of Zürich/Switzerland

2010 - 2013   Spokesman (together with Prof. Hartmut Oschkinat) of the Forschergruppe "Interfering with intracellular protein-protein interactions - probing protein functions with small molecules" (FG 806)
2008 - 2009   Spokesman of the “Zukunftsforum” of the Dechema (Gesellschaft für Chemische Technik und Biotechnologie e. V.

  1. Kuropka, B., Witte, A., Sticht, J., Waldt, N., Majkut, P., Hackenberger, C. P. R., Schraven, B., Krause, E., Kliche, S., and Freund, C. (2015). Analysis of phosphorylation-dependent protein interactions of ADAP reveals novel interaction partners required for chemokine-directed T cell migration. Mol. Cell. Proteom. 14, 2961-72.
  2. Morrison, E., Kuropka, B., Kliche, S., Brügger, B., Krause, E. and Freund, C. (2015). Quantitative analysis of the human T cell palmitome. Sci. Rep. 5, 11598.
  3. Albert, G. I., Schell, C., Kirschner, K. M., Schäfer, S., Naumann, R., Müller, A., Kretz, O., Kuropka, B., Hübner, N., Girbig, M., Krause, E., Scholz, H., Huber, T., Knobeloch, K.-P. and Freund, C. (2015). The GYF domain protein CD2BP2 is critical for embryogenesis and podocyte function. J. Mol. Cell Biol. 7, 402-414.
  4. Schlundt, A., Günther, S., Sticht, J., Wieczorek, M., Roske, Y., Heinemann, U. & Freund, C. (2012). Peptide linkage to the alpha-subunit of MHCII creates a stably inverted antigen presentation complex. J. Mol. Biol. 423, 294-302.
  5. Günther S, Schlundt A, Sticht J, Roske Y, Heinemann U, Wiesmüller KH, Jung G, Falk K, Rötzschke O, and Freund C. (2010) Bidirectional binding of CLIP peptides to an MHC class II molecule. Proc Natl Acad Sci U.S.A. 107, 22219-22224.
  6. Ash, M.-R., Fälber, K., Kosslick, D., Albert, G.I., Roske, Y., Kofler, M., Schümann, M., Krause, E. & Freund, C. (2010). Conserved β-hairpin recognition by the GYF domains of SMY2 and GIGYF2 in mRNA surveillance and vesicular transport complexes. Structure 18, 944-954.
  7. Schlundt, A., Kilian, W., Beyermann, M., Sticht, J., Günther, S., Höpner, S., Falk, K., Rötzschke, O., Mitschang, L. and Freund, C. (2009). A Xenon-129 biosensor for monitoring MHC-peptide interactions. Angew. Chem. Int. Ed. 48, 4142-5.
  8. Piotukh, K., Kosslick, D., Zimmermann, J., Krause, E. & Freund, C. (2007). Reversible disulfide bond formation of intracellular proteins probed by NMR spectroscopy. Free Rad. Biol. Med. 43, 1263-70.
  9. Freund, C., Kühne, R., Yang, H., Park, S., Reinherz, E.L. and Wagner, G. (2002) Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules. EMBO J. 21, 5985-5995.
  10. Freund, C., Dötsch, V., Nishizawa, K., Reinherz, E. & Wagner, G. (1999). The GYF domain is a novel structural fold that is involved in lymphoid signaling through proline-rich sequences. Nat. Struct. Biol. 6, 656-67.