Evidence map›Paper›PMID 33195416›Full record

ArticleFrontiers in molecular biosciences2020

A Not Obvious Correlation Between the Structure of Green Fluorescent Protein Chromophore Pocket and Hydrogen Bond Dynamics: A Choreography From

Federico Coppola, Fulvio Perrella, Alessio Petrone, Greta Donati, Nadia Rega

Abstract read
In one paragraph

Article in Frontiers in molecular biosciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

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  6. Atomic electronegativity-dependent intramolecular hydrogen bond and fluorescence characteristics of novel scaffold-based fluorophore: a TD-DFT study.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
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  12. Editorial: Mechanisms of Fluorescent Proteins.Frontiers in molecular biosciences · 2021
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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.

Federico CoppolaDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Fulvio PerrellaDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Alessio PetroneDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Greta DonatiDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy.
Nadia RegaDepartment of Chemical Sciences, University of Naples Federico II, Naples, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Green Fluorescent Protein (GFP) is a widely studied chemical system both for its large amount of applications and the complexity of the excited state proton transfer responsible of the change in the protonation state of the chromophore. A detailed investigation on the structure of the chromophore environment and the influence of chromophore form (either neutral or anionic) on it is of crucial importance to understand how these factors could potentially influence the protein function. In this study, we perform a detailed computational investigation based on the analysis of

Indexed as

ab initio molecular dynamicsfluorescent proteinshydrogen bond dynamicsQM/MMstructure-function correlation

Identifiers

PMID33195416
PMCPMC7653547

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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.