Pictures

The copyright of all pictures shown on this site is held by J. Kästner. They may be used in talks, as long as a reference to the name or the site is given. Use in any printed material is subject to explicit permission by the owner.

The tunneling path is temperature-dependent. The blue curve indicates the most-likely path of a classical system (displayed below) from one minimum over an energy-barrier to a different one. The yellow, orange, and red paths show the most-likely tunneling paths at decreasing temperature. The thickness of the path below the barrier indicates the quantum mechanical probability of finding the molecule in this stage.

Conformational flexibility and possible agglomeration of epidermal growth factor receptor (EGFR, ErbB1, Her1). Studied by atomistic and coarse-grained molecular dynamics.

Schematic drawing of epidermal growth factor receptor (EGFR, ErbB1, Her1) molecules on a lipid bilayer. A tetramer (front), two dimers (right) and a monomer in its tethered form (left background) are shown.

The active catalytic subunit of Protein Kinase A (surface representation), a substrate (blue ribbon) and ATP (ball-and-stick). Coordinates obtained from PDB entry 1CDK.

Fluorinase is an enzyme that takes fluorine ions and converts them to organo-flouro compounds. We performed QM/MM free-energy perturbation calculations on this system.

The enzyme PHBH takes part in the metabolism of aromatic compounds. The image shows the protein, its active center, and a shell of water molecules as used in a QM/MM setup. We used PHBH mainly to validate QM/MM methods on a real-world system.

Sample potential showing the minimum-energy path obtained with the nudged-elastic band method as implemented in DL-FIND. Red spheres show minima, the blue sphere shows a transition state.