Research interests

  • Signal transduction
  • Membrane protein expression
  • Ion transfer of membrane proteins
  • Photosensory processes
  • Membrane protein folding
  • Interaction of proteins

Research Units in UniSysCat

Dr. Ramona Schlesinger
FU Berlin, Department of Physics: Genetic Biophysics
Arnimallee 14
14195 Berlin
+49 (0)30 838-56249
+49 (0)30 838-56510
r.schlesinger(at)fu-berlin.de
www.physik.fu-berlin.de/en

Publications (selection)

M. Saita, F. Pranga-Sellnau, T. Resler, R. Schlesinger, J. Heberle, V. A. Lórenz-Fonfría, Photoexcitation of the P4480 state induces a secondary photocycle that potentially desensitizes channelrhodopsin-2,
 Journal of the American Chemical Society 2018, 140, 9899-9903.

P. Volz, N. Krause, J. Balke, C. Schneider, M. Walter, F. Schneider, R. Schlesinger, U. Alexiev, Light and pH-induced Changes in Structure and Accessibility of Transmembrane Helix B and Its Immediate Environment in Channelrhodopsin-2,The Journal of Biological Chemistry 2016, 291 (33), 17382-93.


C. Schnedermann, V. Muders, D. Ehrenberg, R. Schlesinger, P. Kukura, J. Heberle, Vibronic Dynamics of the Ultrafast all-trans to 13-cis Photoisomerization of Retinal in Channelrhodopsin-1, Journal of the American Chemical Society 2016, 138, 4757-62. 

V. A. Lorenz-Fonfria, C. Bamann, T. Resler, R. Schlesinger, E. Bamberg, J. Heberle, Temporal evolution of helix hydration in a light-gated ion channel correlates with ion conductance, 
Proceedings of the National Academy of Sciences of the United States of America 2015, 112, E5796-804.

J. Granzin, A. Stadler, A.Cousin, R.Schlesinger, R. Batra-Safferling, 
Structural evidence for the role of polar core residue Arg175 in arrestin activation, Scientific Reports 2015, 5, 15808.

K. Kirchberg, T. Y. Kim, M. Moller, D. Skegro, G. Dasara Raju, J. Granzin, G. Buldt, R. Schlesinger, U. Alexiev, 
Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process, Proceedings of the National Academy of Sciences of the United States of America 2011, 108, 18690-5.

X. Jiang, E. Zaitseva, M. Schmidt, F. Siebert, M. Engelhard, R. Schlesinger, K. Ataka, R. Vogel, J. Heberle, Resolving voltage-dependent structural changes of a membrane photoreceptor by surface-enhanced IR difference spectroscopy,  Proceedings of the National Academy of Sciences of the United States of America 2008, 105, 12113-7.

V. I. Gordeliy, J. Labahn, R. Moukhametzianov, R. Efremov, J. Granzin, R. Schlesinger, G. Buldt, T. Savopol, A. J. Scheidig, J. P. Klare, M. Engelhard, Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex, 
Nature 2002, 419, 484-7.

H. J. Sass, G. Büldt, R. Gessenich, D. Hehn, D. Neff, R. Schlesinger, J. Berendzen, P. Ormos, 
Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin, Nature 2000, 406, 649-53.  

B. Schulz, F. Banuett, M. Dahl, R. Schlesinger, W. Schafer, T. Martin, I. Herskowitz, R. Kahmann, The b alleles of U. maydis, whose combinations program pathogenic development, code for polypeptides containing a homeodomain-related motif, Cell 1990, 60, 295-306.