File:Molecular-Dynamics-Simulations-of-the-Bacterial-UraA-H+-Uracil-Symporter-in-Lipid-Bilayers-Reveal-a-pcbi.1004123.s014.ogv

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Original file (Ogg Theora video file, length 12 s, 960 × 928 pixels, 10.21 Mbps, file size: 14.68 MB)

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English: Self-assembly of POPC lipids around the UraA transporter. In this 100 ns CG-MD simulation the protein Cα atoms were restrained but the side chains were free to rotate and move. The POPC lipids are shown in bond format and the protein in VDW format. The lipid bilayer assembled around the protein very rapidly (after the first ∼15 ns of the simulation), confirming that UraA contains a hydrophobic belt occupied by detergent in the crystal structure.
Date
Source S1 Video from Kalli A, Sansom M, Reithmeier R (2015). "Molecular Dynamics Simulations of the Bacterial UraA H+-Uracil Symporter in Lipid Bilayers Reveal a Closed State and a Selective Interaction with Cardiolipin". PLOS Computational Biology. DOI:10.1371/journal.pcbi.1004123. PMID 25729859. PMC: 4346270.
Author Kalli A, Sansom M, Reithmeier R
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This file is licensed under the Creative Commons Attribution 4.0 International license.
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This file was transferred to Wikimedia Commons from PubMed Central by way of the Open Access Media Importer.
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Date/TimeThumbnailDimensionsUserComment
current21:37, 18 March 201512 s, 960 × 928 (14.68 MB)Open Access Media Importer Bot (talk | contribs)Automatically uploaded media file from Open Access source. Please report problems or suggestions here.

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