Evidence map›Paper›PMID 37047378›Full record

ArticleInternational journal of molecular sciences2023

Crystal Structure of Bright Fluorescent Protein BrUSLEE with Subnanosecond Fluorescence Lifetime; Electric and Dynamic Properties.

Ekaterina Goryacheva, Roman Efremov, Nikolai Krylov, Igor Artemyev, Alexey Bogdanov, Anastasia Mamontova, Sergei Pletnev, Nadya Pletneva, Vladimir Pletnev

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Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 2 countries.

Ekaterina GoryachevaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.ORCID 0009-0005-4636-3530
Roman EfremovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.ORCID 0000-0002-5474-4721
Nikolai KrylovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.ORCID 0000-0002-4520-0351
Igor ArtemyevShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.
Alexey BogdanovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.
Anastasia MamontovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.ORCID 0000-0002-9255-6350
Sergei PletnevVaccine Research Center, National Institute of Allergy and Infectious Diseases, NIH, Bethesda, MD 20892, USA.
Nadya PletnevaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.
Vladimir PletnevShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Ulitsa Miklukho-Maklaya, 16/10, 117997 Moscow, Russia.ORCID 0000-0003-1453-6597
Institute of Bioorganic Chemistry · RUNational Institute of Allergy and Infectious Diseases · USNational Research University Higher School of Economics · RU

Funding

Russian Science Foundation 23-24-00011
6 · The paper itself

Abstract

The rapid development of new microscopy techniques for cell biology has exposed the need for genetically encoded fluorescent tags with special properties. Fluorescent biomarkers of the same color and spectral range and different fluorescent lifetimes (FLs) became useful for fluorescent lifetime image microscopy (FLIM). One such tag, the green fluorescent protein BrUSLEE (Bright Ultimately Short Lifetime Enhanced Emitter), having an extremely short subnanosecond component of fluorescence lifetime (FL~0.66 ns) and exceptional fluorescence brightness, was designed for FLIM experiments. Here, we present the X-ray structure and discuss the structure-functional relations of BrUSLEE. Its development from the EGFP (enhanced green fluorescent proteins) precursor (FL~2.83 ns) resulted in a change of the chromophore microenvironment due to a significant alteration in the side chain conformations. To get further insight into molecular details explaining the observed differences in the photophysical properties of these proteins, we studied their structural, dynamic, and electric properties by all-atom molecular-dynamics simulations in an aqueous solution. It has been shown that compared to BrUSLEE, the mobility of the chromophore in the EGFP is noticeably limited by nonbonded interactions (mainly H-bonds) with the neighboring residues.

Indexed as

Coloring AgentsFluorescenceGreen Fluorescent ProteinsMicroscopy, FluorescenceColoring AgentsGreen Fluorescent Proteinscomputer modelingfluorescence lifetimefluorescent proteinmolecular dynamicsX-ray structure

Identifiers

PMID37047378
PMCPMC10094611
OpenAlexW4361290391

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