ArticleMethodsX2019
Methods toward simplification of time resolved fluorescence anisotropy in proteins labeled with NBD (4-chloro-7-nitrobenzofurazan) adducts.
Article in MethodsX, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed, 1 citations in OpenAlex.
- Nucleotide-mediated modulation of chemoselective protein functionalization in a liquid-like condensed phase.Communications chemistry · 2024Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The analysis of time resolved fluorescence anisotropy for NBD tagged proteins is difficult when multiple exponential components arise from heterogeneous amino acid fluorescent adducts. Two approaches were taken toward simplification. First, N terminal selective labeling of tear lipocalin with NBD-Cl was attempted at pH 7.0. While lysines were predominantly labeled at pH 8.0, selective N terminal labeling was attained at neutral pH. Second, fluorescence anisotropic decay analysis was simplified to recover only the rotational correlation time of the protein not the side chain. The boundaries for analysis of anisotropic decays were limited to the longer lifetimes. A modified tail fit enabled fitting the anisotropic decay to a single exponential. The correlation time for tear lipocalin matched published values. Additionally, a method for normalization of acquisition times of vertically (VV) and horizontally (VH) polarized fluorescence emission decays is presented for time-resolved anisotropy. Here it is applied to Picoharp software (Picoquant, Berlin). Picoharp software is programmed with an automatic stop at unequal acquisition times if the fluorescent counts exceeds a default. The method adjusts the intensity decays to the same acquisition time and is applicable to all time-resolved anisotropic decay data collected with time-correlated photon counting. •NBD labeling at pH 7.0 was not selective for N terminus of LCN1.•Constraints for range simplifies fittings of anisotropic decays.•Different acquisition times for decays can be normalized to facilitate fitting in data obtained by Picoharp.
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