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Fluorescence Anisotropy to Detect In Vivo Stimulus-Induced Changes in Chemoreceptor Packing

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Bacterial Chemosensing

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1729))

Abstract

The anisotropy of the fluorescence emitted from fluorescent proteins, such as yellow fluorescent protein (YFP), is sensitive to Homo-FRET between the proteins. This effect can be used to detect in vivo ligand-induced changes in packing or conformation of tagged chemoreceptors. Such measurements of clustered or dispersed core-signaling units revealed quantitative dose-dependent responses of these sensors.

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Acknowledgment

The use of fluorescence anisotropy for detecting chemoreceptor responses was pioneered in the lab of Howard C. Berg [5]. This work was funded by Israel Science Foundation.

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Correspondence to Ady Vaknin .

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Frank, V., Vaknin, A. (2018). Fluorescence Anisotropy to Detect In Vivo Stimulus-Induced Changes in Chemoreceptor Packing. In: Manson, M. (eds) Bacterial Chemosensing. Methods in Molecular Biology, vol 1729. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7577-8_20

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  • DOI: https://doi.org/10.1007/978-1-4939-7577-8_20

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-7576-1

  • Online ISBN: 978-1-4939-7577-8

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