File:Allosteric-Communication-in-Myosin-V-From-Small-Conformational-Changes-to-Large-Directed-Movements-pcbi.1000129.s001.ogv
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Size of this JPG preview of this OGG file: 680 × 600 pixels. Other resolutions: 272 × 240 pixels | 544 × 480 pixels | 871 × 768 pixels | 1,052 × 928 pixels.
Original file (Ogg Theora video file, length 6.4 s, 1,052 × 928 pixels, 2.44 Mbps, file size: 1.85 MB)
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DescriptionAllosteric-Communication-in-Myosin-V-From-Small-Conformational-Changes-to-Large-Directed-Movements-pcbi.1000129.s001.ogv |
English: The NMSM transition pathway. The movie shows the rigor to post-rigor transition as described by the optimal superposition of the 40 lowest-frequency rigor modes. The rigor (thick tube) and the post-rigor (thin tube) structures are shown in colors and grey, respectively. The color code is as follows: the N, U50, L50, and C/IQ subdomains are colored in orange, blue, red, and lime, respectively; the P-loop, switch I, switch II, SH1 helix, and loop 76–81 connectors are colored in cyan, magenta, yellow, wheat, and pink. The movie shows a coordinated motion of the myosin motor subdomains in which the nucleotide-binding elements (P-loop and switch I) approach the binding site, the lever-arm is displaced downward, and the U50/L50 cleft opens. |
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Source | Video S1 from Cecchini M, Houdusse A, Karplus M (2008). "Allosteric Communication in Myosin V: From Small Conformational Changes to Large Directed Movements". PLOS Computational Biology. DOI:10.1371/journal.pcbi.1000129. PMID 18704171. PMC: 2497441. | ||
Author | Cecchini M, Houdusse A, Karplus M | ||
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Date/Time | Thumbnail | Dimensions | User | Comment | |
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current | 17:42, 16 November 2012 | 6.4 s, 1,052 × 928 (1.85 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 | Cecchini M, Houdusse A, Karplus M |
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Usage terms | http://creativecommons.org/licenses/by/3.0/ |
Image title | The NMSM transition pathway. The movie shows the rigor to post-rigor transition as described by the optimal superposition of the 40 lowest-frequency rigor modes. The rigor (thick tube) and the post-rigor (thin tube) structures are shown in colors and grey, respectively. The color code is as follows: the N, U50, L50, and C/IQ subdomains are colored in orange, blue, red, and lime, respectively; the P-loop, switch I, switch II, SH1 helix, and loop 76?81 connectors are colored in cyan, magenta, yellow, wheat, and pink. The movie shows a coordinated motion of the myosin motor subdomains in which the nucleotide-binding elements (P-loop and switch I) approach the binding site, the lever-arm is displaced downward, and the U50/L50 cleft opens. |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2008-08 |