File:Unfolding-Simulations-Reveal-the-Mechanism-of-Extreme-Unfolding-Cooperativity-in-the-Kinetically-pcbi.1000689.s007.ogv
Unfolding-Simulations-Reveal-the-Mechanism-of-Extreme-Unfolding-Cooperativity-in-the-Kinetically-pcbi.1000689.s007.ogv (Ogg Theora video file, length 2 min 49 s, 280 × 240 pixels, 1.53 Mbps, file size: 30.84 MB)
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[edit]DescriptionUnfolding-Simulations-Reveal-the-Mechanism-of-Extreme-Unfolding-Cooperativity-in-the-Kinetically-pcbi.1000689.s007.ogv |
English: The entire 500K1 unfolding trajectory. The molecule is colored blue at the N-terminus and progressing to red at the C-terminus. Conformations every 2ps are shown. The TSE occurs near the 30 second point in this video. |
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Source | Video S1 from Salimi N, Ho B, Agard D (2010). "Unfolding Simulations Reveal the Mechanism of Extreme Unfolding Cooperativity in the Kinetically Stable α-Lytic Protease". PLOS Computational Biology. DOI:10.1371/journal.pcbi.1000689. PMID 20195497. PMC: 2829044. | ||
Author | Salimi N, Ho B, Agard D | ||
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Date/Time | Thumbnail | Dimensions | User | Comment | |
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current | 19:53, 30 October 2012 | 2 min 49 s, 280 × 240 (30.84 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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Author | Salimi N, Ho B, Agard D |
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Usage terms | http://creativecommons.org/licenses/by/3.0/ |
Image title | The entire 500K1 unfolding trajectory. The molecule is colored blue at the N-terminus and progressing to red at the C-terminus. Conformations every 2ps are shown. The TSE occurs near the 30 second point in this video. |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2010-02 |