Professor, Director at the Max Planck Institute for Biophysical Chemistry

• 1994 Dr. rer nat. (Physics), Technical University of Munich


• 1997 EMBO fellow at the Institute for Molecular Biology and Biophysics, Federal Institute of Technology (ETH) Zurich, Switzerland


• 1998 - 2003 Head of the Theoretical Molecular Biophysics Group at the Max Planck Institute for Biophysical Chemistry, Göttingen


• 2003 Associate Professor for Biomolecular Sciences at the École Polytechnique Fédérale de Lausanne (EPFL)


• 2003- Director at the Max Planck Institute for Biophysical Chemistry, Göttingen, Head of the Theoretical and Computational Molecular Biophysics Department


• 2005- Honorary Professor for Physics at the University of Göttingen

Major Research Interests

The question 'How do proteins work?' is our driving force. We study biomolecular dynamics and function by atomistic molecular dynamics and qm/mm simulations. Emphasis is on protein function, as well as on protein/DNA/RNA interactions.

Available projects address nuclear pore transport, the ribosome, molecular motors such as F-ATPase (figure 1), protein unfolding as well as the interaction with radiation with a focus at single molecules, typically in close collaboration with experimental groups. The simulation of single molecule AFM experiments by force probe techniques helps us to reveal mechanisms of proteins function involving mechanical stress such as the muscular force sensor titin kinase (figure 2), and so do improved methods to calculate thermodynamic quantities from simulations. We are continuously advancing our simulation techniques and scalability on massively parallel computers. The group of ca. 20 PhD students and postdocs shares a strong background mainly in physics, and scientific computing, but also in chemistry and biology. We enjoy exclusive access to a high-performance linux cluster of ca. 3000 processor cores (figure 3).







Homepage Department / Research Group

http://www.mpibpc.mpg.de/home/grubmueller/index.html



Selected Recent Publications

• Zachariae, U. and Grubmüller, H. (2006) A Highly Strained Nuclear Conformation of the Exportin Cse1p Revealed by Molecular Dynamics Simulations. Structure 14, 1469-1478


• Gräter, F., Shen, J., Jiang, H., Gautel, M. and H. Grubmüller (2005) Mechanically Induced Titin Kinase Activation Studied by Force-Probe Molecular Dynamics Simulations. Biophys. J. 88, 790-804


• Lange, O.F. and Grubmüller, H. and B.L. de Groot (2005) Molecular Dynamics Simulations of Protein G Challenge NMR-Derived Correlated Backbone Motions. Angew. Chem. Int. Ed.: 44, 3394-3399


• Andresen, M., Wahl, M.C. , Stiel, A.C., Gräter, F., Schäfer, L.V., Trowitzsch, S., Weber, G., Eggeling, C., Grubmüller, H., Hell, S.W. and Jakobs, S. (2005) Structure and mechanism of the reversible photoswitch of a fluorescent protein. PNAS 102, 13070-13074


• Böckmann, R.A. and Grubmüller, H. (2004) Multistep Binding of Divalent Cations to Phospholipid Bilayers: A Molecular Dynamics Study. Angew. Chemie Int. Ed. 43, 1021-1024


• de Groot, B.L., Frigato, T., Helms, V. and H. Grubmüller (2003) The mechanism of proton exclusion in the aquaporin-1 water channel. J. Mol.Biol. 333, 279-293


• Margittai, M., Widengren, J., Schweinberger, E., Schröder, G.F., Fasshauer, D., Felekyan, S., Haustein, E., König, M., Grubmüller, H., Jahn, R. and Seidel, C. A. M. (2003) Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of syntaxin 1. PNAS 100, 15516


• Böckmann, R. and Grubmüller, H. (2002) Nanoseconds molecular dynamics simulation of primary mechanical energy transfer steps in F1-ATP synthase, Nature Struct. Biol. 9, 198


• de Groot, B.L. and Grubmüller, H. (2001) Water Permeation Across Biological Membranes: Mechanism and Dynamics of Aquaporin-1 and GlpF, Science 294, 2353


• Heymann, B. and Grubmüller, H. (2000) Dynamic force spectroscopy of molecular adhesion bonds. Phys. Rev. Lett. 84, 6126-6129