File:Dual-Chaperone-Role-of-the-C-Terminal-Propeptide-in-Folding-and-Oligomerization-of-the-Pore-Forming-ppat.1002135.s005.ogv

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.
Date
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/TimeThumbnailDimensionsUserComment
current01:41, 18 November 201242 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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Format Bitrate Download Status Encode time
VP9 480P 1.02 Mbps Completed 22:40, 24 August 2018 1 min 8 s
Streaming 480p (VP9) 1.02 Mbps Completed 23:11, 5 February 2024 1.0 s
VP9 360P 589 kbps Completed 22:40, 24 August 2018 50 s
Streaming 360p (VP9) 589 kbps Completed 05:31, 7 February 2024 1.0 s
VP9 240P 315 kbps Completed 22:40, 24 August 2018 45 s
Streaming 240p (VP9) 316 kbps Completed 06:40, 17 December 2023 1.0 s
WebM 360P 514 kbps Completed 01:47, 18 November 2012 48 s
Streaming 144p (MJPEG) 1.02 Mbps Completed 04:59, 9 November 2023 2.0 s

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