Evidence map›Paper›PMID 29706225›Full record

ArticleBiophysical journal2018

Photophysical Behavior of mNeonGreen, an Evolutionarily Distant Green Fluorescent Protein.

Frederik Steiert, Eugene P Petrov, Peter Schultz, Petra Schwille, Thomas Weidemann

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.6field-weighted citation impact, top 7% of its field
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

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.

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

19 citing papers in PubMed, 41 citations in OpenAlex.

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  13. A genetically encoded BRET-based SARS-CoV-2 MCommunications chemistry · 2022
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  18. Superfolder mTurquoise2Molecular microbiology · 2019
    Article
  19. Article
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

5 authors at 1 institution in 1 country.

Frederik SteiertDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany; Physics Department, Technical University Munich, Garching, Germany.
Eugene P PetrovDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany; Faculty of Physics, Ludwig Maximilian University of Munich, Munich, Germany.
Peter SchultzDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Petra SchwilleDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany.
Thomas WeidemannDepartment of Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Martinsried, Germany. Electronic address: weidemann@biochem.mpg.de.
Max Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent proteins (FPs) feature complex photophysical behavior that must be considered when studying the dynamics of fusion proteins in model systems and live cells. In this work, we characterize mNeonGreen (mNG), a recently introduced FP from the bilaterian Branchiostoma lanceolatum, in comparison to the well-known hydrozoan variants enhanced green fluorescent protein (EGFP) and Aequorea coerulescens GFP by steady-state spectroscopy and fluorescence correlation spectroscopy in solutions of different pH. Blind spectral unmixing of sets of absorption spectra reveals three interconverting electronic states of mNG: a nonfluorescent protonated state, a bright state showing bell-shaped pH dependence, and a similarly bright state dominating at high pH. The gradual population of the acidic form by external protonation is reflected by increased flickering at low pH in fluorescence correlation spectroscopy measurements, albeit with much slower flicker rates and lower amplitudes as compared to Aequorea GFPs. In addition, increased flickering of mNG indicates a second deprotonation step above pH 10 leading to a slight decrease in fluorescence. Thus, mNG is distinguished from Aequorea GFPs by a two-step protonation response with opposite effects that reflects a chemically distinct chromophore environment. Despite the more complex pH dependence, mNG represents a superior FP under a broad range of conditions.

Indexed as

Evolution, MolecularAnimalsGreen Fluorescent ProteinsHydrogen-Ion ConcentrationLanceletsSpectrometry, FluorescenceGreen Fluorescent Proteins

Identifiers

PMID29706225
PMCPMC6129466
OpenAlexW2789851401

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.