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File:Corresponding-Functional-Dynamics-across-the-Hsp90-Chaperone-Family-Insights-from-a-Multiscale-pcbi.1002433.s017.ogv

Corresponding-Functional-Dynamics-across-the-Hsp90-Chaperone-Family-Insights-from-a-Multiscale-pcbi.1002433.s017.ogv ‎(Ogg Theora video file, length 0.0 s, 688 × 512 pixels, 0 bps, file size: 12.22 MB)

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English: Solid backbone: Grp94 meta-trajectory. The meta-trajectory consists of all protomeric snapshots (restricted to the 525 amino acids alignable with Hsp90 and HtpG) of Grp94 in the Apo, ADP- and ATP-bound states. The faint backbone represents the best fit to the Grp94 protomers obtained by suitably rotating the two terminal quasi-rigid domains of protomeric template (see Figure 6) around the axes shown as cyan cylinders.
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Source Video S1 from Morra G, Potestio R, Micheletti C, Colombo G (2012). "Corresponding Functional Dynamics across the Hsp90 Chaperone Family: Insights from a Multiscale Analysis of MD Simulations". PLOS Computational Biology. DOI:10.1371/journal.pcbi.1002433. PMID 22457611. PMC: 3310708.
Author Morra G, Potestio R, Micheletti C, Colombo G
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current21:42, 17 November 20120.0 s, 688 × 512 (12.22 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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VP9 480P 0 bps Completed 20:42, 22 August 2018 1 min 8 s
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