Detecting in-solution conformational changes in viral fusogens using tryptophan-induced fluorescence quenching.
| Autor: | Serrão VHB; Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, Canada., Lee JE; Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, ON M5S 1A8, Canada. |
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| Jazyk: | angličtina |
| Zdroj: | STAR protocols [STAR Protoc] 2021 Dec 06; Vol. 2 (4), pp. 100994. Date of Electronic Publication: 2021 Dec 06 (Print Publication: 2021). |
| DOI: | 10.1016/j.xpro.2021.100994 |
| Abstrakt: | Dynamic monitoring of protein conformational changes is necessary to fully understand many biological processes. For example, viral entry and membrane fusion require rearrangement of its viral glycoprotein. We present a step-by-step protocol for site-specific bimane labeling of the influenza-C fusogen to map proximity and conformational movements using tryptophan-induced fluorescence quenching. This protocol is adaptable for other proteins and for protein-protein interaction detection. For complete details on the use and execution of this protocol, please refer to Serrão et al., 2021. Competing Interests: The authors declare no competing interests. (© 2021 The Author(s).) |
| Databáze: | MEDLINE |
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