File:Electrostatically-Biased-Binding-of-Kinesin-to-Microtubules-pbio.1001207.s007.ogv
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Electrostatically-Biased-Binding-of-Kinesin-to-Microtubules-pbio.1001207.s007.ogv (Ogg Theora video file, length 32 s, 550 × 550 pixels, 1.93 Mbps, file size: 7.28 MB)
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[edit]DescriptionElectrostatically-Biased-Binding-of-Kinesin-to-Microtubules-pbio.1001207.s007.ogv |
English: A typical Brownian dynamics simulation. The simulation is initiated with kinesin and tubulin in random orientations and positions on the “initiation sphere,” where electrostatic energy contours are centrosymmetric. At large distances both proteins will undergo free diffusion leading to possible “escape.” At closer distances each protein will start to experience the electrostatic field of the other protein. Eventually, kinesin and tubulin will be close enough to favorably orient themselves with respect to their electrostatic fields. Note that in the simulations, both proteins are freely diffusing; here, for clarity, the camera tracks around the tubulin heterodimer. |
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Source | Movie S3 from Grant B, M. Gheorghe D, Zheng W, Alonso M, Huber G, Dlugosz M, McCammon J, Cross R (2011). "Electrostatically Biased Binding of Kinesin to Microtubules". PLOS Biology. DOI:10.1371/journal.pbio.1001207. PMID 22140358. PMC: 3226556. | ||
Author | Grant B, M. Gheorghe D, Zheng W, Alonso M, Huber G, Dlugosz M, McCammon J, Cross R | ||
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Date/Time | Thumbnail | Dimensions | User | Comment | |
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current | 16:45, 30 October 2012 | 32 s, 550 × 550 (7.28 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 | Grant B, M. Gheorghe D, Zheng W, Alonso M, Huber G, Dlugosz M, McCammon J, Cross R |
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Usage terms | http://creativecommons.org/licenses/by/3.0/ |
Image title | A typical Brownian dynamics simulation. The simulation is initiated with kinesin and tubulin in random orientations and positions on the ?initiation sphere,? where electrostatic energy contours are centrosymmetric. At large distances both proteins will undergo free diffusion leading to possible ?escape.? At closer distances each protein will start to experience the electrostatic field of the other protein. Eventually, kinesin and tubulin will be close enough to favorably orient themselves with respect to their electrostatic fields. Note that in the simulations, both proteins are freely diffusing; here, for clarity, the camera tracks around the tubulin heterodimer. |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2011-11 |