Mr. Sven Schünke

Photo of Sven  Schünke

Sven Schünke

Willbold Group
Institute of Molecular Biophysics II
Research Center Jülich GmbH
Leo Brandt Straße
Building: 05.2
Floor/Room: 2009
Phone +492461-61-2117

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • BSc (intermediate diploma) in Biology, 2003, Heinrich-Heine-University, Düsseldorf, Germany

Second degree and/or intermediate examination:

  • MSc (diploma) in Biology, 2005, Heinrich-Heine-University, Düsseldorf, Germany


  • Schünke S, Novak K, Stoldt M, Kaupp UB, Willbold D (2007): Resonance assignment of the cyclic nucleotide binding domain from a cyclic nucleotide-gated K+ channel in complex with cAMP. Biomol. NMR Assign. 1(2):179-181
  • Schünke S, Stoldt M, Novak K, Kaupp UB, Willbold D (2009): Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP. EMBO Rep. 10(7): 729-735 (doi:10.1038/embor.2009.68)
  • Schünke S, Schünke S, Lecher J, Stoldt M, Kaupp UB, Willbold D (2010): Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain. Biomol. NMR Assign. 4(2):147-150
  • Schünke S, Stoldt M, Lecher J, Kaupp UB, Willbold D (2011) Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. Proc. Natl. Acad. Sci. U S A 108(15):6121-6126 (doi:10.1073/pnas.1015890108)

Attended conferences:

  • International School on High Field NMR-Spectroscopy for Solids and Liquids, 14.-19.05.2006, Institut de Biologie Structurale Jean-Pierre Ebel, Grenoble, France
  • XXIInd International Conference on Magnetic Resonance in Biological Systems, 20.-25.08.2006, Göttingen, Germany
  • Murnau Conference, 'Structural Biology of Disease Mechanisms', 05.-08.09.2007, Murnau, Germany
  • First Annual Meeting, bio-N3MR Network NRW, 10.10.2007, Jülich, Germany
  • Extend-NMR Meeting, 'New Approaches to Biomolecular Structure Determination', 27.-29.10.2008, Berlin, Germany
  • Second Annual Meeting, bio-N3MR Network NRW, 13.11.2008, Jülich, Germany
  • Elite-Netzwerk Bayern Graduate School, 'Structure in Biology ' Key to Understanding', 21.-26.09.2008, Bayreuth, Germany
  • Research Center caesar, 15.01.2009, Bonn, Germany
  • 50th ENC "Experimental Nuclear Magnetic Resonance Conference", 29.03.-03.04.2009, Student Travel Stipend, (Pacific Grove, California, USA)
  • BioStruct Master Class: "Approaches to Determine Protein Structures", 06.-09.07.2010, Heinrich-Heine-Universität Düsseldorf, Germany
  • BioScience 2010: "Workshop on Expanding the Frontiers of Biomolecular Science", 15.-17.11.2010, Jülich, Germany
  • Keystone Conference "Transmembrane Signaling by GPCRs and Channels", 23.-28.01.2011, Taos, New Mexico, USA
  • International Magnetic Resonance Conference "EUROMAR 2011", 21.-25.08.2011, Goethe-Universität Frankfurt am Main


  • From 11/2008 to 07/2010: Full scholarship of the NRW-Research School BioStruct, Heinrich Heine University, Düsseldorf, Germany
  • Poster prize for the NMR study "Structural basis of cyclic nucleotide-activated ion channel gating" at International Magnetic Resonance Conference "EUROMAR 2011", Frankfurt

BioStruct PhD project

Structural Studies of a Cyclic Nucleotide-Activated Potassium Channel Binding Domain in Solution by Nuclear Magnetic Resonance (NMR) Spectroscopy
Ion channels activated by cyclic nucleotides play key roles in neuronal excitability and signal transduction of visual and olfactory neurons. They belong to two subfamilies: Cyclic nucleotide-gated (CNG) channels, and hyperpolarization-activated and cyclic nucleotidegated (HCN) channels (Kaupp & Seifert, 2001, 2002). Both channel types share a carboxyterminal cyclic nucleotide-binding domain (CNBD). HCN channels are activated by hyperpolarization and their activity is modulated by cyclic nucleotides. In contrast, CNG channels are voltage independent and require cyclic nucleotides to open. Binding of cyclic nucleotides promotes the opening of the channel. Probably, a conformational change in the CNBD is propagated to the pore. However, the mechanism by which the binding of cyclic nucleotides to the CNBD leads to the opening of the channel is not well understood. Therefore we initiated the structural characterization of the CNBD in solution by Nuclear Magnetic Resonance (NMR) spectroscopy in order to get insights into the "gating" mechanism of such channel types.


Topic Supervisor:

undefinedProf. Dr. Dieter Willbold, Institute for Physical Biology, Willbold Group

Complementary Supervisor:

undefinedProf. Dr. Lutz Schmitt, Institute for Biochemistry, Schmitt Group

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