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Forschungszentrum Jülich - FZJ


Multifold functionality and structure

Research at the Institute of Complex Systems (Structural Biochemistry, ICS-6) focusses on the investigation of three-dimensional structures and interactions of proteins, to elucidate how biological macromolecules perform their multitude of functions in cells and organism. Furthermore, the institute investigates pathways of misfolding and subsequent loss or gain of function, with the focus on proteins involved in the development and progression of neurodegenerative diseases like Alzheimer’s and Parkinson’s disease. Based on these insights the ICS-6 is developing new approaches for diagnosis and therapy, including their validation in vitro and in vivo. Scientists from a variety of disciplines like biochemistry, biology, chemistry, medicine, pharmacy and physics work together within the institutes’ interdisciplinary projects.

Successful progression of the research projects requires a wide array of methods from molecular biology and biophysics, as well as an excellent infrastructure of scientific large scale facilities. Highly sensitive, innovative and efficient methods from molecular biology, protein chemistry, biophysics, spectroscopy and microscopy are used in state-of-the-art lab spaces (security levels S1, S2 and S3**).

A particular strength is the development and application of nuclear magnetic resonance (NMR) spectroscopy for protein structure and dynamics investigation. Together with the Institute of Physical Biology at Heinrich-Heine-University Düsseldorf, the ICS-6 is running the Biomolecular NMR Center. Situated in Jülich, it hosts several high-field solution and solid state NMR devices in the range from 600 to 900 MHz, making it one of Germany’s leading NMR centers. In the coming years, the addition of a 800 MHz widebore DNP-NMR-Spectrometer and a 1.2 gigahertz NMR spectrometer will lead to a further increase in sensitivity and resolution, thereby establishing Jülich as an internationally unique location for NMR based structural biology.

To ensure access to the most suitable methods and infrastructures in all areas of structural biology research, the ICS-6 is engaged in strong collaborations on the local, national and international level. Cutting-edge equipment for X-ray crystallography is available, including measuring times at synchrotron beamlines, as well as access to neutron sources and supercomputers.

The broad expertise and excellent technological environment at ICS-6 provide ideal conditions to meet today’s most pressing challenges in health research.Insights provided by structural biology and their implementation in applied research go hand in hand.

View of the 900 MHz NMR device of the Biomolecular NMR Center. Inside, the magnetic field strength is 21 Tesla and allows highly sensitive NMR experiments to elucidate the 3D structures and dynamics of proteins and their complexes with drugs and other ligands. The Biomolecular NMR Center currently hosts three 600 MHz-NMR-Spectrometers, two devices with 800 and 900 MHz respectively and a 600 MHz DNP-NMR-Spectrometer.

Forschungszentrum Jülich

The ICS-6 is part of the Institute of Complex Systems at Forschungszentrum Jülich. With more than 5,500 employees, Jülich – a member of the Helmholtz Association – is one of the large interdisciplinary research centres in Europe, pursuing cutting-edge interdisciplinary research on pressing issues facing society today. With its competence in materials science and simulation, and its expertise in physics, nanotechnology, and information technology, as well as in the biosciences and brain research, Jülich is developing the basis for the key technologies of tomorrow. In this way, Forschungszentrum Jülich helps to solve the grand challenges facing society in the fields of energy and the environment as well as information and the brain. Forschungszentrum Jülich is also breaking new ground in the form of strategic partnerships with universities, research institutions, and industry in Germany and abroad.



Granzin J, Stadler A, Cousin A, Schlesinger R, Batra-Safferling R; Structural evidence for the role of polar core residue Arg175 in arrestin activation. Scientific Reports 2015 Oct 29;5:15808. doi: 10.1038/srep15808 PubMed

Brener O, Dunkelmann T, Gremer L, van Groen T, Mirecka EA, Kadish I, Willuweit A, Kutzsche J, Jürgens D, Rudolph S, Tusche M, Bongen P, Pietruszka J, Oesterhelt F, Langen K-J, Demuth H-U, Janssen A, Hoyer W, Funke SA, Nagel-Steger L, Willbold D; QIAD assay for quantitating a compound’s efficacy in elimination of toxic Aβ oligomers. Sci. Rep. 5, 13222; doi: 10.1038/srep13222 (2015).

Michel M, Schwarten M, Decker C, Nagel-Steger L, Willbold D, Weiergräber OH; The mammalian autophagy initiator complex contains two HORMA domain proteins. Autophagy 2015 Nov;11(12):2300-8. doi: 10.1080/15548627.2015.1076605. PubMed

Ma P, Xue Y, Coquelle N, Haller JD, Yuwen T, Ayala I, Mikhailovskii O, Willbold D, Colletier J-P, Skrynnikov NR, Schanda P; Observing the overall rocking motion of a protein in a crystal. Nat. Commun. 6, 8361 (2015) DOI: 10.1038/ncomms9361 PubMed

Braun T, Orlova A, Valegard K, Lindas AC, Schröder GF, Egelman EH; An Archaeal Actin from a Hyperthermophile Forms a Single-Stranded Filament. PNAS, DOI: 10.1073/pnas.1509069112. PubMed

Shaykhalishahi H, Gauhar A, Wördehoff MM, Grüning CS, Klein A, Bannach O, Stoldt M, Willbold D, Härd T, Hoyer W; Contact between the beta1 and beta2 segments of alpha-synuclein that inhibits amyloid formation. Angew. Chem. Int. Ed. 54, 8837-8840 (2015) PubMed

Gushchin I, Shevchenko V, Polovinkin V, Kovalev K, Alekseev A, Round E, Borshchevskiy V, Balandin T, Popov A, Gensch T, Fahlke C, Bamann C, Willbold D, Büldt G, Bamberg E, Gordeliy V; Crystal structure of a light-driven sodium pump. Nat. Struct. Mol. Biol. 22, 390-395 (2015) doi:10.1038/nsmb.3002

Müller H, Brener O, Andreoletti O, Piechatzek T, Willbold D, Legname G, Heise H; Progress toward structural understanding of infectious sheep PrP-amyloid. Prion 8, 344-358 (2014) DOI:10.4161/19336896.2014.983754

Kowal J, Chami M, Baumgartner P, Arheit M, Chiu PL, Rangl M, Scheuring S, Schröder GF, Nimmigean CM, Stahlberg H; Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1. Nat Commun 5, 3106 (2014) [10.1038/ncomms4106]

Lu A, Magupalli VG, Ruan J, Yin Q, Atianand MK, Vos M, Schröder GF, Fitzgerald KA, Wu H, and Egelman EH; Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes. Cell 156, 1193-1206 (2014) dx.doi.org/10.1016/j.cell.2014.02.008


Mirecka EA, Shaykhalishahi H, Gauhar A, Akgül S, Lecher J, Willbold D, Stoldt M, Hoyer W. Sequestration of a beta-hairpin for control of alpha-synuclein aggregation
Angew. Chem. Int. Ed. 53, 4227-4230 (2014).


Ma P, Schwarten M, Schneider L, Boeske A, Henke N, Lisak D, Weber S, Mohrlüder J, Stoldt M, Strodel B, Methner A, Hoffmann S, Weiergräber OH, Willbold D
Interaction of Bcl-2 with the autophagy-related GABAA receptor-associated protein (GABARAP): Biophysical characterization and functional implications.
J. Biol. Chem. 288, 37204-37215 (2013).



Schünke S, Stoldt M, Lecher J, Kaupp UB, Willbold D. Structural insights into conformational changes of a cyclic nucleotide-binding domain in solution from Mesorhizobium loti K1 channel. Proc. Natl. Acad. Sci. USA, 108, 6121-6126 (2011).


Schwarten M, Mohrlüder J, Ma P, Stoldt M, Thielmann Y, Stangler T, Hersch N, Hoffmann B, Merkel R, Willbold D. Nix directly binds to GABARAP: A possible crosstalk between apoptosis and autophagy. Autophagy 5, 690-698 (2009).

Schünke S, Stoldt M, Novak K, Kaupp UB, Willbold D. Solution structure of the M.loti K1 channel cyclic nucleotide binding domain in complex with cAMP. EMBO Rep. 10, 729-735 (2009).




Prof. Dr. Dieter Willbold
Direktor ICS-6

Forschungszentrum Juelich
ICS-6: Strukturbiochemie
D-52425 Jülich

Heinrich-Heine-Universität Düsseldorf
Institut für Physikalische Biologie
D-40225 Düsseldorf
  +49 211 811 1390