File:A-programmable-DNA-origami-nanospring-that-reveals-force-induced-adjacent-binding-of-myosin-VI-heads-ncomms13715-s4.ogv
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A-programmable-DNA-origami-nanospring-that-reveals-force-induced-adjacent-binding-of-myosin-VI-heads-ncomms13715-s4.ogv (Ogg Theora video file, length 8.0 s, 44 × 35 pixels, 65 kbps, file size: 64 KB)
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[edit]DescriptionA-programmable-DNA-origami-nanospring-that-reveals-force-induced-adjacent-binding-of-myosin-VI-heads-ncomms13715-s4.ogv |
English: Supplementary Movie 2 A nanospring was fluorescently labeled by thirteen TAMRA-labeled staple strands, and immobile myosin II and single myosin VI were attached to the ends. Non-fluorescent actin filaments were adsorbed on the cover glass, and the nanospring-motor protein complex was tethered to the actin via immobile myosin IIs. Myosin VI tethered with the nanospring moved processively along actin filaments, and the stretch/compression dynamics of a fluorescently labeled nanospring could be seen by TIRF microscopy (10 Hz frame rate, ×10 play). See also Fig. 2d. |
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Source | Video file from Iwaki M, Wickham S, Ikezaki K, Yanagida T, Shih W (2016). "A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads". Nature Communications. DOI:10.1038/ncomms13715. PMID 27941751. PMC: 5159853. | ||
Author | Iwaki M, Wickham S, Ikezaki K, Yanagida T, Shih W | ||
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This file is licensed under the Creative Commons Attribution 4.0 International license.
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current | 05:47, 1 February 2017 | 8.0 s, 44 × 35 (64 KB) | 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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Short title | Supplementary Movie 2 |
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Author | Iwaki M, Wickham S, Ikezaki K, Yanagida T, Shih W |
Usage terms | http://creativecommons.org/licenses/by/4.0/ |
Image title | A nanospring was fluorescently labeled by thirteen TAMRA-labeled staple strands, and immobile myosin II and single myosin VI were attached to the ends. Non-fluorescent actin filaments were adsorbed on the cover glass, and the nanospring-motor protein complex was tethered to the actin via immobile myosin IIs. Myosin VI tethered with the nanospring moved processively along actin filaments, and the stretch/compression dynamics of a fluorescently labeled nanospring could be seen by TIRF microscopy (10 Hz frame rate, ×10 play). See also Fig. 2d. |
Software used | Xiph.Org libtheora 1.1 20090822 (Thusnelda) |
Date and time of digitizing | 2016-12-12 |