Structural and Computational Study of the GroEL - Prion Protein complex
Authors/Creators
- 1. Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia
- 2. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia
- 3. National Research Center «Kurchatov Institute», Moscow, Russia
- 4. Faculty of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Moscow, Russia
Description
Data for Publication "Structural and Computational Study of the GroEL - Prion Protein complex".
Starting structures of the GroEL-PrP(N) and GroEL-PrP(C) complexes in .pdb format (without water molecules and ions).
Video S1: ISAC 2d classes showing the mobility of the PrP inside the GroEL cavity.
Video S2: The course of MD trajectories with GroEL-PrP(N) complex. Proteins are shown with tube representation using VMD program (version 1.9.4a12): grey - GroEL, blue - PrP N-terminal domain, red - PrP C-terminal domain. Only the Cα atoms of both proteins are shown for clarity. The trajectory is shown with 250 ps timestep, with a smoothing window size of 10 for GroEL and 5 for PrP.
Video S3: The course of MD trajectories with GroEL-PrP(C) complex. Proteins are shown with tube representation using VMD program (version 1.9.4a12): grey - GroEL, blue - PrP N-terminal domain, red - PrP C-terminal domain. Only the Cα atoms of both proteins are shown for clarity. The trajectory is shown with 250 ps timestep, with a smoothing window size of 10 for GroEL and 5 for PrP.
