Heisenberg Fellow of the DFG at the Max-Planck-Institute for Biophysical Chemistry

• 1990 - 1996 Studies at the Ludwig Maximilians University of Munich, Degree: Diploma in Physics (passed with distinction)


• 1993 - 1994 Studies at the University of Edinburgh, Scotland; Physics and Russian


• 1996 - 1998 PhD project with Dr. Tad Holak, Max-Planck-Institute for Biochemistry, Martinsried


• 1998 Degree Dr. rer. nat., Technical University of Munich


• 1998 - 1999 Postdoctoral Fellow at the Max-Planck-Institute for Biochemistry (Dr. Tad Holak)


• 1999 - 2001 Postdoctoral Fellow at the National Institutes of Health, Bethesda, USA (group of Dr. A. Bax)


• since 2001 Emmy-Noether Group Leader at the Max-Planck-Institute for Biophysical Chemistry, Göttingen


• since 2007 Heisenberg Fellow of the DFG


• since 2008 Honorary Professor, University of Göttingen

Major Research Interests

The goal of our research is to push NMR spectroscopy into new research areas and to provide insights at the molecular level into the factors that are responsible for the neurotoxicity of the proteins alpha-synuclein, Tau and Amyloid-beta peptide during the course of Parkinson’s and Alzheimer’s disease. In addition, we strive to obtain structure-function relationships for integral membrane proteins, such as the human voltage dependent anion channel.


Homepage Department/Research Group

http://www.mpibpc.mpg.de/research/ags/zweckstetter/index.html



Selected Recent Publications

• Bibow S, Mukrasch MD, Chinnathambi S, Biernat J, Griesinger C, Mandelkow E, Zweckstetter M.Angew Chem Int Ed Engl. (2011) The Dynamic Structure of Filamentous Tau. Oct 11. .Angew Chem Int Ed Engl.



• Villinger, S., Briones, R., Giller, K., Zachariae, U., Lange, A., de Groot, B. L., Griesinger, C., Becker, S. and Zweckstetter, M. (2010) Functional dynamics in the voltage-dependent anion channel. Proc Natl Acad Sci U S A 107, 22546-22551



• Kim, H. Y., Cho, M. K., Kumar, A., Maier, E., Siebenhaar, C., Becker, S., Fernandez, C. O., Lashuel, H. A., Benz, R., Lange, A., and Zweckstetter, M.* (2009) Structural properties of pore-forming oligomers of alpha-synuclein. J Am Chem Soc 131, 17482-17489



• Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., and Zweckstetter, M. (2009). Structural polymorphism of 441-residue tau at single residue resolution. PLoS Biol 7, e34.



• Bayrhuber, M., Meins, T., Habeck, M., Becker, S., Giller, K., Villinger, S., Vonrhein, C., Griesinger, C., Zweckstetter, M., and Zeth, K. (2008). Structure of the human voltage-dependent anion channel. Proc Natl Acad Sci U S A 105, 15370-15375.



• Kim, H. Y., Cho, M. K., Riedel, D., Fernandez, C. O., and Zweckstetter, M. (2008). Dissociation of amyloid fibrils of alpha-synuclein in supercooled water. Angew Chem Int Ed Engl 47, 5046-5048.



• Zweckstetter, M. (2008). NMR: prediction of molecular alignment from structure using the PALES software. Nat Protoc 3, 679-690.



• Korukottu, J., Bayrhuber, M., Montaville, P., Vijayan, V., Jung, Y. S., Becker, S., and Zweckstetter, M. (2007). Fast high-resolution protein structure determination by using unassigned NMR data. Angew Chem Int Ed Engl 46, 1176-1179.



• Cho, M. K., Kim, H. Y., Bernado, P., Fernandez, C. O., Blackledge, M., and Zweckstetter, M. (2007). Amino acid bulkiness defines the local conformations and dynamics of natively unfolded alpha-synuclein and tau. J Am Chem Soc 129, 3032-3033.



• Skora, L., Cho, M. K., Kim, H. Y., Becker, S., Fernandez, C. O., Blackledge, M., and Zweckstetter, M. (2006). Charge-induced molecular alignment of intrinsically disordered proteins. Angew Chem Int Ed Engl 45, 7012-7015.



• Iwahara, J., Zweckstetter, M., and Clore, G. M. (2006). NMR structural and kinetic characterization of a homeodomain diffusing and hopping on nonspecific DNA. Proc Natl Acad Sci U S A 103, 15062-15067.



• Bertoncini, C. W., Jung, Y. S., Fernandez, C. O., Hoyer, W., Griesinger, C., Jovin, T. M., and Zweckstetter, M. (2005). Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein. Proc Natl Acad Sci U S A 102, 1430-1435.