File:Dual-Chaperone-Role-of-the-C-Terminal-Propeptide-in-Folding-and-Oligomerization-of-the-Pore-Forming-ppat.1002135.s005.ogv
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Dual-Chaperone-Role-of-the-C-Terminal-Propeptide-in-Folding-and-Oligomerization-of-the-Pore-Forming-ppat.1002135.s005.ogv (Ogg Theora video file, length 42 s, 640 × 480 pixels, 2.6 Mbps, file size: 13.16 MB)
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English: Molecular dynamics simulation of aerolysin WT without the CTP. Result of a molecular dynamics simulation of aerolysin WT with CTP manually removed. The secondary structure of every frame, as calculated by the DSSP algorithm, is represented in the cartoon with different colors: yellow is beta sheet; white and cyan are random coil; purple and blue are alpha helix. Two strands unfold from Domain 4 in the direction of the loop region in Domain 3. |
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| Source | Video S2 from Iacovache I, Degiacomi M, Pernot L, Ho S, Schiltz M, Dal Peraro M, van der Goot F (2011). "Dual Chaperone Role of the C-Terminal Propeptide in Folding and Oligomerization of the Pore-Forming Toxin Aerolysin". PLOS Pathogens. DOI:10.1371/journal.ppat.1002135. PMID 21779171. PMC: 3136475. | ||
| Author | Iacovache I, Degiacomi M, Pernot L, Ho S, Schiltz M, Dal Peraro M, van der Goot F | ||
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| Date/Time | Thumbnail | Dimensions | User | Comment | |
|---|---|---|---|---|---|
| current | 01:41, 18 November 2012 | 42 s, 640 × 480 (13.16 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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