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• W3202017758 abstract "Abstract Genetically encoded potassium indicators lack optimal binding affinity for monitoring intracellular dynamics in mammalian cells. Through structure-guided design and genome mining of potassium binding proteins, we developed green fluorescent potassium indicators with a broad range of binding affinities. KRaION1, based on the insertion of a potassium binding protein (Ec-Kbp) into the fluorescent protein mNeonGreen, exhibits an isotonically measured K d of 69±10 (mM; mean ± standard deviation used throughout). We identified Ec-Kbp’s binding site using NMR spectroscopy to detect protein-thallium scalar couplings and refined the structure of Ec-Kbp in its potassium-bound state. Guided by this structure, we modified KRaION1, yielding KRaION2, which exhibits an isotonically measured K d of 96±9 (mM). We identified four Ec-Kbp homologs as potassium binding proteins, which yielded indicators with isotonically measured binding affinities in the 39-112 (mM) range. KRaIONs expressed and functioned in HeLa cells, but exhibited lower K d values, which were mirrored by lower K d values measured in vitro when holding sodium constant. Thus, potassium indicator K d may need to be evaluated in the context of a given experimental goal." @default.
• W3202017758 created "2021-10-11" @default.
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• W3202017758 date "2021-10-08" @default.
• W3202017758 modified "2023-09-27" @default.
• W3202017758 title "Tuning the sensitivity of genetically encoded fluorescent potassium indicators through structure-guided and genome mining strategies" @default.
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• W3202017758 doi "https://doi.org/10.1101/2021.10.07.463355" @default.
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