Evidence map›Paper›PMID 36555282›Full record

ArticleInternational journal of molecular sciences2022

Direct or Indirect ESPT Mechanism in CFP psamFP488? A Theoretical-Computational Investigation.

Greta Donati, Nadia Rega

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

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

2 authors.

Greta DonatiDepartment of Chemical Sciences, University of Napoli Federico II, Complesso Universitario di M.S. Angelo, Via Cintia 21, I-80126 Napoli, Italy.ORCID 0000-0002-0311-1721
Nadia RegaDepartment of Chemical Sciences, University of Napoli Federico II, Complesso Universitario di M.S. Angelo, Via Cintia 21, I-80126 Napoli, Italy.ORCID 0000-0002-2983-766X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent Proteins are widely studied for their multiple applications in technological and biotechnological fields. Despite this, they continue to represent a challenge in terms of a complete understanding of all the non-equilibrium photo-induced processes that rule their properties. In this context, a theoretical-computational approach can support experimental results in unveiling and understanding the processes taking place after electronic excitation. A non-standard cyan fluorescent protein, psamFP488, is characterized by an absorption maximum that is blue-shifted in comparison to other cyan fluorescent proteins. This protein is characterized by an extended Stokes shift and an ultrafast (170 fs) excited state proton transfer. In this work, a theoretical-computational study, including excited state ab initio dynamics, is performed to help understanding the reaction mechanism and propose new hypotheses on the role of the residues surrounding the chromophore. Our results suggest that the proton transfer could be indirect toward the acceptor (Glu167) and involves other residues surrounding the chromophore, despite the ultrafast kinetics.

Indexed as

ProtonsGreen Fluorescent ProteinsGreen Fluorescent ProteinsProtonsexcited state ab initio molecular dynamicsfluorescent proteinsphoto-induced proton transfer

Identifiers

PMID36555282
PMCPMC9779432

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Registered trials

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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.