File:Identification-of-the-Allosteric-Regulatory-Site-of-Insulysin-pone.0020864.s013.ogv
Size of this JPG preview of this OGG file: 800 × 450 pixels. Other resolutions: 320 × 180 pixels | 640 × 360 pixels | 1,280 × 720 pixels.
Original file (Ogg Theora video file, length 4.0 s, 1,280 × 720 pixels, 830 kbps, file size: 405 KB)
File information
Structured data
Captions
Summary
editDescriptionIdentification-of-the-Allosteric-Regulatory-Site-of-Insulysin-pone.0020864.s013.ogv |
English: Dimer conformational change. The enzyme dimer is shown in a backbone representation converting from the wild type unliganded form to the rIDE-E111F liganded form. The orientation is the same as that in the upper image of Fig. S1 panel A. |
||
Date | |||
Source | Movie S2 from Noinaj N, Bhasin S, Song E, Scoggin K, Juliano M, Juliano L, Hersh L, Rodgers D (2011). "Identification of the Allosteric Regulatory Site of Insulysin". PLOS ONE. DOI:10.1371/journal.pone.0020864. PMID 21731629. PMC: 3123307. | ||
Author | Noinaj N, Bhasin S, Song E, Scoggin K, Juliano M, Juliano L, Hersh L, Rodgers D | ||
Permission (Reusing this file) |
|
||
Provenance InfoField |
|
File history
Click on a date/time to view the file as it appeared at that time.
Date/Time | Thumbnail | Dimensions | User | Comment | |
---|---|---|---|---|---|
current | 13:03, 18 November 2012 | 4.0 s, 1,280 × 720 (405 KB) | Open Access Media Importer Bot (talk | contribs) | Automatically uploaded media file from Open Access source. Please report problems or suggestions here. |
You cannot overwrite this file.
File usage on Commons
There are no pages that use this file.
Transcode status
Update transcode statusMetadata
This file contains additional information such as Exif metadata which may have been added by the digital camera, scanner, or software program used to create or digitize it. If the file has been modified from its original state, some details such as the timestamp may not fully reflect those of the original file. The timestamp is only as accurate as the clock in the camera, and it may be completely wrong.
Author | Noinaj N, Bhasin S, Song E, Scoggin K, Juliano M, Juliano L, Hersh L, Rodgers D |
---|---|
Usage terms | http://creativecommons.org/licenses/by/3.0/ |
Image title | Dimer conformational change. The enzyme dimer is shown in a backbone representation converting from the wild type unliganded form to the rIDE-E111F liganded form. The orientation is the same as that in the upper image of Fig. S1 panel A. |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2011 |