Movies
Ubiquitin Allostery
C.A. Smith et al.: PNAS USA 113,3269-3274 (2016)
For movies related to the April 2017 MPIbpc News article about Ubiquitin allostery, please click here.
Cover caption: Allosterically regulated, sub-angstrom contraction of ubiquitin enables binding to USP deubiquitinases (yellow).
Aquaporin
B.L. de Groot and H. Grubmüller: Science 294,2353-2357 (2001)
Aquaporin-1 in action. Simulation fragment of 200 ps of aquaporin-1. Generated using Molscript/Bobscript and raster3d. Click here for a higher resolution version.Pathway of a water molecule through AQP1. Ribbon representation of one aquaporin-1 monomer and a selection of water molecules. One water molecule, coloured yellow, finds its way completely through the pore. Those sidechains that are in direct contact with passing water molecules are shown explicitly. Movie made with Molscript/Bobscript and raster3d. Click here for a higher resolution version.
Images
Aquaporin
B.L. de Groot and H. Grubmüller: Science 294,2353-2357 (2001)
The periodic simulation system for Aquaporin-1 The protein is active as a tetramer (the monomers are depicted in orange/cyan/magenta/blue), embedded in a lipid bilayer membrane (yellow/green) surrounded by water molecules (red/white). The system size is approx. 100.000 atoms; all simulations were performed with full electroststics and had a length of 10 ns. Picture made with Molscript/Bobscript and raster3d.Aquaporin-1 in action. Snapshot of aquaporin-1 during the MD simulation, as water molecules diffuse through the pores. Picture made with Molscript/Bobscript and raster3d. Click here for a MPEG movie of a trajectory fragment of 200 ps.
Pathway of a water molecule through AQP1. Surface representation of one aquaporin-1 monomer and, superimposed, overlaid snapshots of a water molecule on its way through the pore. The regions of the protein that interact strongest with passing water molecules are shown in yellow. Picture made with Dino.
Pathway of a water molecule through AQP1. Ribbon representation of one aquaporin-1 monomer and, superimposed, overlaid snapshots of a water molecule on its way through the pore. Those sidechains that are in direct contact with passing water molecules are shown explicitly. Picture made with Molscript/Bobscript and raster3d. Click here for a MPEG movie of a permeation event in a 2 ns trajectory fragment (watch the yellow water molecule).
Water dipole distribution in AQP1. Ribbon representation of one aquaporin-1 monomer and, superimposed, the average dipole moment of water molecules passing the pore. The water dipole rotates by about 180 degrees on passing the pore. The protein is coloured according to the local electrostatic potential. Picture made with Molscript/Bobscript and raster3d.
Superimposed trajectories of water molecules through the aquaporin-1 pores. In the ten nanoseconds that were simulated, 16 full permeation events were observed, in good agreement with the experimental rate. Picture made with Molscript/Bobscript and raster3d.