Evidence map›Paper›PMID 32499507›Full record

ArticleNature communications2020

Geometric and electronic structure probed along the isomerisation coordinate of a photoactive yellow protein chromophore.

Cate S Anstöter, Basile F E Curchod, Jan R R Verlet

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

4 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Excited-State Barrier ControlsThe journal of physical chemistry letters · 2022
    Article
  4. 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

3 authors at 1 institution in 1 country.

Cate S AnstöterDepartment of Chemistry, Durham University, Durham, DH1 3LE, UK.ORCID http://orcid.org/0000-0002-3412-2511
Basile F E CurchodDepartment of Chemistry, Durham University, Durham, DH1 3LE, UK.ORCID http://orcid.org/0000-0002-1705-473X
Jan R R VerletDepartment of Chemistry, Durham University, Durham, DH1 3LE, UK. j.r.r.verlet@durham.ac.uk.ORCID http://orcid.org/0000-0002-9480-432X
Durham University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding the connection between the motion of the nuclei in a molecule and the rearrangement of its electrons lies at the heart of chemistry. While many experimental methods have been developed to probe either the electronic or the nuclear structure on the timescale of atomic motion, very few have been able to capture both these changes in concert. Here, we use time-resolved photoelectron imaging to probe the isomerisation coordinate on the excited state of an isolated model chromophore anion of the photoactive yellow protein. By probing both the electronic structure changes as well as nuclear dynamics, we are able to uniquely measure isomerisation about a specific bond. Our results demonstrate that the photoelectron signal dispersed in time, energy and angle combined with calculations can track the evolution of both electronic and geometric structure along the adiabatic state, which in turn defines that chemical transformation.

Indexed as

ElectronsAnisotropyBacterial ProteinsIsomerismPhotoreceptors, MicrobialTime FactorsBacterial Proteinsphotoactive yellow protein, BacteriaPhotoreceptors, Microbial

Identifiers

PMID32499507
PMCPMC7272410
OpenAlexW3033971153

What OpenQuestion holds

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LicenceCC BY
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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.