Wikipedia

Hartmut Oschkinat

Hartmut Oschkinat (born 28 February 1957)[1] is a German structural biologist and professor for chemistry at the Free University of Berlin. His research focuses on the study of biological systems with solid-state nuclear magnetic resonance.

Hartmut Oschkinat
Oschkinat in 2016
Born (1957-02-28) 28 February 1957 (age 67)
NationalityGerman
CitizenshipGerman
Alma materGoethe University Frankfurt
AwardsGünther Laukien Prize
Scientific career
InstitutionsFMP Berlin
Free University of Berlin
Thesis Analysis of the conformation of Cyclosporin in solution using NMR-spectroscopy: development and use of new methods  (1986)
Doctoral advisorHorst Kessler
Websitewww.leibniz-fmp.de/research/structuralbiology/researchgroups/oschkinat/intro.html

He is a member of the Editorial Boards of the Journal of Biomolecular NMR and Structure.[2][3]

Life and career

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Oschkinat studied chemistry at the Johann-Wolfgang-Goethe University of Frankfurt. He received his doctoral degree in 1986 under the supervision of Horst Kessler with the title "Analysis of the conformation of Cyclosporin in solution using NMR-spectroscopy: development and use of new methods." in the field of nuclear magnetic resonance spectroscopy (NMR). After his work as a postdoctoral researcher with Geoffrey Bodenhausen at the University of Lausanne, Oschkinat moved to the Max Planck Institute of Biochemistry in Martinsried in 1987 as a post-doc in the Lab of Marius Clore and Angela Gronenborn. There, he was working with Marius Clore, Angela Gronenborn and the Nobel laureate Robert Huber. After his habilitation at the Technical University of Munich in 1992, Hartmut Oschkinat moved to the European Molecular Biology Laboratory in Heidelberg. Since 1998, he is the head of the department NMR-supported Structural Biology at the Leibniz-Institut für Molekulare Pharmakologie in Berlin.[4]

Research

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At the beginning of his career, Oschkinat worked in the field of solution-state NMR, and made fundamental contributions[5] to establish the role of multidimensional NMR spectroscopy in structural biology. After using solution-state NMR spectroscopy to determine three-dimensional structures of soluble proteins such as the pleckstrin homology domain[6] and the WW domain,[7] characterise protein–protein interactions involving the latter,[8] with applications in fragment-based drug discovery,[9][10] he moved on to focus on the investigation of biological systems by solid-state NMR (ssNMR) with magic angle spinning. His group was the first to solve a protein structure using ssNMR;[11] the structure solved was that of a microcrystalline preparation of a SH3 domain.[12] Since 2005, his research group investigates complex biomolecular systems such as membrane proteins within the native lipid environment,[13][14][15] amyloid fibrils,[16] and oligomers.[17] Moreover, he develops methods to address challenging questions in structural biology where ssNMR can be applied with particular advantages, and have made particular contributions to the development of dynamic nuclear polarisation[18][19] and proton detection using fast magic angle spinning.[20]

Notable Achievements

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References

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  1. ^ "Symposium: Biological Solid-State NMR and Beyond, in honour of Hartmut Oschkinat's 60th birthday". Leibniz-Institut für Molekulare Pharmakologie. Archived from the original (jpg) on 27 February 2017. Retrieved 24 January 2017.
  2. ^ "Editorial Board of Journal of Biomolecular NMR". Retrieved 2017-02-14.
  3. ^ "Staff and Editorial Board of Structure". Retrieved 2017-02-14.
  4. ^ "Department of NMR-Supported Structural biology (Hartmut Oschkinat)". FMP Berlin. Archived from the original on 27 February 2017. Retrieved 25 January 2017.
  5. ^ Oschkinat H, Griesinger C, Kraulis PJ, Sørensen OW, Ernst RR, Gronenborn AM, Clore GM (1988). "Three-dimensional NMR spectroscopy of a protein in solution". Nature. 332 (6162): 374–6. Bibcode:1988Natur.332..374O. doi:10.1038/332374a0. PMID 3352736. S2CID 4261068.
  6. ^ Macias MJ, Musacchio A, Ponstingl H, Nilges M, Saraste M, Oschkinat H (1994). "Structure of the pleckstrin homology domain from beta-spectrin". Nature. 369 (6482): 675–7. Bibcode:1994Natur.369..675M. doi:10.1038/369675a0. PMID 8208297. S2CID 4358947.
  7. ^ Macias MJ, Gervais V, Civera C, Oschkinat H (2000). "Structural analysis of WW domains and design of a WW prototype". Nat. Struct. Biol. 7 (5): 375–9. doi:10.1038/75144. PMID 10802733. S2CID 1328841.
  8. ^ Macias MJ, Hyvönen M, Baraldi E, Schultz J, Sudol M, Saraste M, Oschkinat H (1996). "Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide". Nature. 382 (6592): 646–9. Bibcode:1996Natur.382..646M. doi:10.1038/382646a0. PMID 8757138. S2CID 4306964.
  9. ^ Joshi M, Vargas C, Boisguerin P, Diehl A, Krause G, Schmieder P, Moelling K, Hagen V, Schade M, Oschkinat H (2006). "Discovery of low-molecular-weight ligands for the AF6 PDZ domain". Angew. Chem. Int. Ed. Engl. 45 (23): 3790–5. doi:10.1002/anie.200503965. PMID 16671149.
  10. ^ Pellecchia M, Bertini I, Cowburn D, Dalvit C, Giralt E, Jahnke W, James TL, Homans SW, Kessler H, Luchinat C, Meyer B, Oschkinat H, Peng J, Schwalbe H, Siegal G (2008). "Perspectives on NMR in drug discovery: a technique comes of age". Nat Rev Drug Discov. 7 (9): 738–45. doi:10.1038/nrd2606. PMC 2891904. PMID 19172689.
  11. ^ Comellas G, Rienstra CM (2013). "Protein structure determination by magic-angle spinning solid-state NMR, and insights into the formation, structure, and stability of amyloid fibrils". Annu Rev Biophys. 42: 515–36. doi:10.1146/annurev-biophys-083012-130356. PMID 23527778.
  12. ^ Castellani F, van Rossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H (2002). "Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy". Nature. 420 (6911): 98–102. Bibcode:2002Natur.420...98C. doi:10.1038/nature01070. PMID 12422222. S2CID 4422584.
  13. ^ Hiller M, Krabben L, Vinothkumar KR, Castellani F, van Rossum BJ, Kühlbrandt W, Oschkinat H (2005). "Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli". ChemBioChem. 6 (9): 1679–84. doi:10.1002/cbic.200500132. PMID 16138308. S2CID 39312280.
  14. ^ Krabben L, van Rossum BJ, Jehle S, Bocharov E, Lyukmanova EN, Schulga AA, Arseniev A, Hucho F, Oschkinat H (2009). "Loop 3 of short neurotoxin II is an additional interaction site with membrane-bound nicotinic acetylcholine receptor as detected by solid-state NMR spectroscopy". J. Mol. Biol. 390 (4): 662–71. doi:10.1016/j.jmb.2009.05.016. PMID 19447114.
  15. ^ Shahid SA, Bardiaux B, Franks WT, Krabben L, Habeck M, van Rossum BJ, Linke D (2012). "Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals". Nat. Methods. 9 (12): 1212–7. doi:10.1038/nmeth.2248. PMID 23142870. S2CID 5089257.[permanent dead link‍]
  16. ^ Ferguson N, Becker J, Tidow H, Tremmel S, Sharpe TD, Krause G, Flinders J, Petrovich M, Berriman J, Oschkinat H, Fersht AR (2006). "General structural motifs of amyloid protofilaments". Proc. Natl. Acad. Sci. U.S.A. 103 (44): 16248–53. Bibcode:2006PNAS..10316248F. doi:10.1073/pnas.0607815103. PMC 1637568. PMID 17060612.
  17. ^ Jehle S, Rajagopal P, Bardiaux B, Markovic S, Kühne R, Stout JR, Higman VA, Klevit RE, van Rossum BJ, Oschkinat H (2010). "Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers". Nat. Struct. Mol. Biol. 17 (9): 1037–42. doi:10.1038/nsmb.1891. PMC 2957905. PMID 20802487.
  18. ^ Geiger MA, Orwick-Rydmark M, Märker K, Franks WT, Akhmetzyanov D, Stöppler D, Zinke M, Specker E, Nazaré M, Diehl A, van Rossum BJ, Aussenac F, Prisner T, Akbey Ü, Oschkinat H (2016). "Temperature dependence of cross-effect dynamic nuclear polarization in rotating solids: advantages of elevated temperatures". Phys Chem Chem Phys. 18 (44): 30696–30704. Bibcode:2016PCCP...1830696G. doi:10.1039/c6cp06154k. PMID 27791210.
  19. ^ Stöppler D, Song C, van Rossum BJ, Geiger MA, Lang C, Mroginski MA, Jagtap AP, Sigurdsson ST, Matysik J, Hughes J, Oschkinat H (2016). "Dynamic Nuclear Polarization Provides New Insights into Chromophore Structure in Phytochrome Photoreceptors". Angew. Chem. Int. Ed. Engl. 55 (52): 16017–16020. doi:10.1002/anie.201608119. PMID 27879035.
  20. ^ Nieuwkoop AJ, Franks WT, Rehbein K, Diehl A, Akbey Ü, Engelke F, Emsley L, Pintacuda G, Oschkinat H (2015). "Sensitivity and resolution of proton detected spectra of a deuterated protein at 40 and 60 kHz magic-angle-spinning". J. Biomol. NMR. 61 (2): 161–71. doi:10.1007/s10858-015-9904-0. PMID 25663049. S2CID 27308791.
  21. ^ "Find people in the EMBO Communities". EMBO. Retrieved 24 January 2017.
  22. ^ "Professor Walter Rosenthal New Scientific Director of the Max Delbrück Center". Health Capital Berlin Brandenburg. 6 January 2009. Retrieved 24 January 2017. Professor Hartmut Oschkinat shall hold the office of Acting Director of the FMP until a successor has been appointed.[permanent dead link‍]
  23. ^ "Volker Haucke ist neuer Direktor des FMP". Forshungsverbund Berlin e.V. 9 January 2012. Archived from the original on 28 February 2017. Retrieved 24 January 2017. ...sagt Prof. Hartmut Oschkinat, der das Institut in den letzten drei Jahren kommissarisch leitete.
  24. ^ "Scientific Evaluation". Central European Institute of Technology. June 2012. Archived from the original on 9 June 2017. Retrieved 24 January 2017.
  25. ^ "CEITEC - Step Forward in Material and Life Sciences" (PDF). Technology Centre CAS. p. 13. Archived from the original (PDF) on 27 December 2019. Retrieved 24 January 2017.
  26. ^ "NMRS Members". National Magnetic Resonance Society of India. Retrieved 27 February 2017.
  27. ^ "Tutorial & Award Lectures". ENC conference. Archived from the original on 27 February 2017. Retrieved 24 January 2017.
  28. ^ "2014 Laukien: Hartmut Oschkinat (Leibniz-Institut, Berlin)". Vimeo. 2015-11-12. Retrieved 24 January 2017.
  29. ^ "Bruker: Laukien Prize was awarded to six solid-state NMR spectroscopists". Bruker. Archived from the original on 27 December 2019. Retrieved 24 January 2017.
  30. ^ "Monday at ENC: Laukien Prize Winners 2014". The Resonance. 2014-03-25. Retrieved 24 January 2017.
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