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You are here: FRIAS Fellows Fellows 2021/22 Prof. Dr. Gerhard Stock

Prof. Dr. Gerhard Stock

University of Freiburg
Internal Senior Fellow
October 2013 - July 2014

Phone +49 761-203 5750


Gerhard Stock was born on April 1st, 1962. In 1987 he received his diploma in Physics at the Technical University of Munich, Germany. From 1986-1990 he worked as a PhD student at the Department of Chemistry, Technical University of Munich, where he completed his PhD (Prof. W. Domcke) in 1990. 1991-1992 Postdoctoral Fellow (Prof. W. H. Miller) at the Dept. of Chemistry, University of California, Berkeley; 1993-1996 Research Associate, Dept. of Chemistry, Technical University of  Munich; 1996 Habilitation (Theoretical Chemistry), Technical University of  Munich;  1997-2000 Heisenberg Professor, Dept. of Physics, University of Freiburg; 2000-2009 C4 Professor, Chair of Theoretical  Chemistry, University of Frankfurt. Since 2009 Gerhard Stock is W3 Professor (Chair of Theoretical Physics) at the University of Freiburg.

Gerhard Stock was awarded the following fellowships and distinctions: 1990 Ph.D. Thesis (summa cum laude); 1991 Postdoctoral Fellowship of the Deutsche Forschungsgemeinschaft (DFG); 1993 Habilitation Fellowship of the Deutsche Forschungsgemeinschaft (DFG); 1997 Heisenberg Prize; 2002 Annual Prize of the International Academy of Quantum Molecular Science. He is referee and member of referee panels of several funding agencies including the Deutsche Forschungsgemeinschaft (DFG), Humboldt Foundation, National Science Foundation, Minerva Foundation, and referee for numerous journals, including Science, PNAS, J. Am. Chem. Soc., Phys. Rev. Letters, Rev. Mod. Phys.

Recent activities: 2011/2012 Director of the Institute of Physics at the University of Freiburg; 2013 Co-organizer of the Black Forest Focus on “Protein Dynamics” at the Freiburg Institute for Advanced Studies (FRIAS) and the Telluride Science Research Center meeting on “Vibrationals Dynamics”.

Fields of Research: Ultrafast Nonadiabatic Dynamics and Spectroscopy; Free Energy Landscapes of Biomolecules; Biomolecular Energy flow; Functional Dynamics; Vibrational Signatures of Biomolecular Dynamics.


Selected Publications

  • Vibrational conical intersections as mechanism of ultrafast vibrational relaxation, P. Hamm and G. Stock, Phys. Rev. Lett. 109, 173201 (2012)


  • Identifying metastable states of folding proteins, A. Jain and G. Stock, J. Comp. Theo. Chem. 8, 3810 (2012)


  • Real Time Observation of Ultrafast Peptide Conformational Dynamics: Molecular  Dynamics Simulation vs Infrared Experiment, P. H. Nguyen, H. Staudt, J. Wachtveitl, and G. Stock, J. Phys. Chem. B 115, 13084 (2011)


  • Classical simulation of quantum energy flow in biomolecules, G. Stock, Phys. Rev. Lett. 102, 118301 (2009)


  • Energy Transport in Peptide Helices, V. Botan, E. Backus, R. Pfister, A. Moretto, M. Crisma, C. Toniolo, P. H. Nguyen, G. Stock, and P. Hamm, Proc. Nat. Acad. Sci. (USA) 104, 12749-12754 (2007)



FRIAS Research Project

Energy and signal flow in proteins

The propagation of energetic and conformational changes in a protein, in other words, energy transfer and intramolecular signaling, plays a vital role in biomolecular function. Picosecond time-resolved infrared experiments on photoswitchable proteins provide a new and promising way to study these processes, the microscopic mechanisms of which are only little understood. To facilitate the interpretations of ongoing experiments on the villin headpiece, the WW domain, and the PDZ2 domain, we will perform extensive molecular dynamics (MD) simulations. Using nonequilibrium MD techniques, we will identify the time scales, efficiency, and pathways of the vibrational energy flow in these model proteins. Intramolecular allosteric interactions or intramolecular signaling will be studied by employing an azobenzene photoswitch, which has the potential to switch between the ligand-bound and ligand-free state of the PDZ2 domain. Extensive MD simulations of the photoinduced conformational change and intramolecular signaling will be conducted that allow us to observe the functioning of the protein in real time. Moreover, we will calculate transient infrared spectra to facilitate the direct comparison to experiment.