File:Compact-Conformations-of-Human-Protein-Disulfide-Isomerase-pone.0103472.s006.ogv
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Compact-Conformations-of-Human-Protein-Disulfide-Isomerase-pone.0103472.s006.ogv (Ogg Theora video file, length 9.6 s, 688 × 544 pixels, 13.09 Mbps, file size: 14.92 MB)
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DescriptionCompact-Conformations-of-Human-Protein-Disulfide-Isomerase-pone.0103472.s006.ogv |
English: Representative movements of the domains of hPDI in Sim 4. With the b domain structurally aligned to the crystal structure, it is clearly shown that domains a and a' become much closer and the overall conformation becomes more compact as time evolves. Cysteine residues at the active sites are indicated as sticks with the sulfur atoms in yellow. |
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Source | Movie S1 from Yang S, Wang X, Cui L, Ding X, Niu L, Yang F, Wang C, Wang C, Lou J (2014). "Compact Conformations of Human Protein Disulfide Isomerase". PLOS ONE. DOI:10.1371/journal.pone.0103472. PMID 25084354. PMC: 4118876. | ||
Author | Yang S, Wang X, Cui L, Ding X, Niu L, Yang F, Wang C, Wang C, Lou J | ||
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This file is licensed under the Creative Commons Attribution 4.0 International license.
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Date/Time | Thumbnail | Dimensions | User | Comment | |
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current | 22:35, 8 August 2014 | 9.6 s, 688 × 544 (14.92 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 | Yang S, Wang X, Cui L, Ding X, Niu L, Yang F, Wang C, Wang C, Lou J |
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Usage terms | http://creativecommons.org/licenses/by/4.0/ |
Image title | Representative movements of the domains of hPDI in Sim 4. With the b domain structurally aligned to the crystal structure, it is clearly shown that domains a and a' become much closer and the overall conformation becomes more compact as time evolves. Cysteine residues at the active sites are indicated as sticks with the sulfur atoms in yellow. |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2014 |