Portrait Hartmut Oschkinat

Prof. Dr.

Hartmut Oschkinat

Head Oschkinat Group

 +49 30 94793 160

 oschkinat@fmp-berlin.de

Structural characterisation of protein-protein interactions responsible for the reception and transduction of signals in biological systems, and their disruption by small molecules. Protein domains which recognize peptides with characteristic motifs, proteins involved in protein homeosthasis, structural investigations on membrane proteins and cytoskeleton-attached proteins by solid state NMR.
More than 180 publications in the fields of protein structure and NMR methods development.  More than 50 structures deposited in the PDB. Among those are first structures of the PH- and WW-domains. Development of small molecular inhibitors of interactions of PDZ domains. First assignment of protein resonances on the basis of solid-state NMR data, first structure of a protein by solid-state NMR. Structure of a fibril formed by a WW-domain at atomic resolution. Structure of alphaB-crystallin oligomers by solid-state NMR and SAXS. Applications of dynamic nuclear polarisation to large biological complexes. Structure of the dark-adapted form of bacteriorhodopsin by solution NMR.


Structural Biology


Oschkinat Group


FMP
FU Berlin

Curriculum Vitae

2009 – 2011

Acting Director

FMP

since 1998

Head of the department "NMR-supported Structural Biology“ at the FMP, Professor of Structural Chemistry at the Free University in Berlin

FMP, FU Berlin

1992 – 1998

Group leader. Work on structure and function of signalling domains

EMBL, Heidelberg

1987 – 1991

Position as NMR-spectroscopist, first in the Clore/Gronenborn group, later independently in the department of Prof. Huber. Pulse sequence development, 3D-NMR

Max-Planck-Institute for Biochemistry (Martinsried)

Publications

of 8

Collective exchange processes reveal an active site proton cage in bacteriorhodopsin

  • Friedrich, D.
  • Brünig, F. N.
  • Nieuwkoop, A. J.
  • Netz, R. R.
  • Hegemann, P., &
  • Oschkinat, H.

Communications Biology 2020, 3, 4

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Crystal structure of Q4D6Q6, a conserved kinetoplastid-specific protein from Trypanosoma cruzi

  • D'Andrea, E. D.
  • Roske, Y.
  • Oliveira, G. A. P.
  • Cremer, N.
  • Diehl, A.
  • Schmieder, P.
  • Heinemann, U.
  • Oschkinat, H., &
  • Pires, J. R.

Journal of Structural Biology 2020, 211, 107536

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Designed nanomolar small-molecule inhibitors of Ena/VASP EVH1 interaction impair invasion and extravasation of breast cancer cells

  • Barone, M.
  • Müller, M.
  • Chiha, S.
  • Ren, J.
  • Albat, D.
  • Soicke, A.
  • Dohmen, S.
  • Klein, M.
  • Bruns, J.
  • Dinther, M.
  • Opitz, R.
  • Lindemann, P.
  • Beerbaum, M.
  • Motzny, K.
  • Roske, Y.
  • Schmieder, P.
  • Volkmer, R.
  • Nazare, M.
  • Heinemann, U.
  • Oschkinat, H.
  • Ten Dijke, P.
  • Schmalz, H. G., &
  • Kühne, R.

Proceedings of the National Academy of Sciences of the United States of America 2020, 117, 29684-29690

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MAS NMR detection of hydrogen bonds for protein secondary structure characterization

  • Friedrich, D.
  • Perodeau, J.
  • Nieuwkoop, A. J., &
  • Oschkinat, H.

Journal of Biomolecular NMR 2020, 74, 247-256

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NMR quality control of fragment libraries for screening

  • Sreeramulu, S.
  • Richter, C.
  • Kuehn, T.
  • Azzaoui, K.
  • Blommers, M. J. J.
  • Del Conte, R.
  • Fragai, M.
  • Trieloff, N.
  • Schmieder, P.
  • Nazare, M.
  • Specker, E.
  • Ivanov, V.
  • Oschkinat, H.
  • Banci, L., &
  • Schwalbe, H.

Journal of Biomolecular NMR 2020, 74, 555-563

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pH-Dependent Protonation of Surface Carboxylate Groups in PsbO Enables Local Buffering and Triggers Structural Changes

  • Gerland, L.
  • Friedrich, D.
  • Hopf, L.
  • Donovan, E. J.
  • Wallmann, A.
  • Erdmann, N.
  • Diehl, A.
  • Bommer, M.
  • Buzar, K.
  • Ibrahim, M.
  • Schmieder, P.
  • Dobbek, H.
  • Zouni, A.
  • Bondar, A. N.
  • Dau, H., &
  • Oschkinat, H.

ChemBioChem 2020, 21, 1597-1604

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Pigmentation Chemistry and Radical-Based Collagen Degradation in Alkaptonuria and Osteoarthritic Cartilage

  • Chow, W. Y.
  • Norman, B. P.
  • Roberts, N. B.
  • Ranganath, L. R.
  • Teutloff, C.
  • Bittl, R.
  • Duer, M. J.
  • Gallagher, J. A., &
  • Oschkinat, H.

Angewandte Chemie-International Edition 2020, 59, 11937-11942

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Protein resonance assignment by BSH-CP based 3D solid-state NMR experiments: A practical guide

  • Hoffmann, J.
  • Ruta, J.
  • Shi, C.
  • Hendriks, K.
  • Chevelkov, V.
  • Franks, W. T.
  • Oschkinat, H.
  • Giller, K.
  • Becker, S., &
  • Lange, A.

Magnetic Resonance in Chemistry 2020, 58, 445-465

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Publications

of 6

Detection of nucleic acids and other low abundance components in native bone and osteosarcoma extracellular matrix by isotope enrichment and DNP-enhanced NMR

  • Goldberga, I.
  • Li, R.
  • Chow, W. Y.
  • Reid, D. G.
  • Bashtanova, U.
  • Rajan, R.
  • Puszkarska, A.
  • Oschkinat, H., &
  • Duer, M. J.

RSC Advances 2019, 9, 26686-26690

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DNP NMR of biomolecular assemblies

  • Jaudzems, K.
  • Polenova, T.
  • Pintacuda, G.
  • Oschkinat, H., &
  • Lesage, A.

Journal of Structural Biology 2019, 206, 90-98

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Dynamic Nuclear Polarization Magic-Angle Spinning Nuclear Magnetic Resonance Combined with Molecular Dynamics Simulations Permits Detection of Order and Disorder in Viral Assemblies

  • Gupta, R.
  • Zhang, H. L.
  • Lu, M. M.
  • Hou, G. J.
  • Caporini, M.
  • Rosay, M.
  • Maas, W.
  • Struppe, J.
  • Ahn, J.
  • Byeon, I. J. L.
  • Oschkinat, H.
  • Jaudzems, K.
  • Barbet-Massin, E.
  • Emsley, L.
  • Pintacuda, G.
  • Lesage, A.
  • Gronenborn, A. M., &
  • Polenova, T.

Journal of Physical Chemistry B 2019, 123, 5048-5058

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Host monitoring of quorum sensing during Pseudomonas aeruginosa infection

  • Moura-Alves, P.
  • Puyskens, A.
  • Stinn, A.
  • Klemm, M.
  • Guhlich-Bornhof, U.
  • Dorhoi, A.
  • Furkert, J.
  • Kreuchwig, A.
  • Protze, J.
  • Lozza, L.
  • Pei, G.
  • Saikali, P.
  • Perdomo, C.
  • Mollenkopf, H. J.
  • Hurwitz, R.
  • Kirschhoefer, F.
  • Brenner-Weiss, G.
  • Weiner, 3.
  • Oschkinat, H.
  • Kolbe, M.
  • Krause, G., &
  • Kaufmann, S. H. E.

Science 2019, 366, eaaw1629

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Poly(ADP-Ribose) Links the DNA Damage Response and Biomineralization

  • Müller, K. H.
  • Hayward, R.
  • Rajan, R.
  • Whitehead, M.
  • Cobb, A. M.
  • Ahmad, S.
  • Sun, M. X.
  • Goldberga, I.
  • Li, R.
  • Bashtanova, U.
  • Puszkarska, A. M.
  • Reid, D. G.
  • Brooks, R. A.
  • Skepper, J. N.
  • Bordoloi, J.
  • Chow, W. Y.
  • Oschkinat, H.
  • Groombridge, A.
  • Scherman, O. A.
  • Harrison, J. A.
  • Verhulst, A.
  • D'Haese, P. C.
  • Neven, E.
  • Needham, L. M.
  • Lee, S. F.
  • Shanahan, C. M., &
  • Duer, M. J.

Cell Reports 2019, 27, 3124-3138

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The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants

  • Kesten, C.
  • Wallmann, A.
  • Schneider, R.
  • McFarlane, H. E.
  • Diehl, A.
  • Khan, G. A.
  • Rossum, B. J.
  • Lampugnani, E. R.
  • Szymanski, W. G.
  • Cremer, N.
  • Schmieder, P.
  • Ford, K. L.
  • Seiter, F.
  • Heazlewood, J. L.
  • Sanchez-Rodriguez, C.
  • Oschkinat, H., &
  • Persson, S.

Nature Communications 2019, 10, 857

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