Evidence map›Paper›PMID 34163965›Full record

ArticleChemical science2020

Reproducibility in the unfolding process of protein induced by an external electric field.

Anna Sinelnikova, Thomas Mandl, Christofer Östlin, Oscar Grånäs, Maxim N Brodmerkel, Erik G Marklund, Carl Caleman

Abstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

7 authors.

Anna SinelnikovaDepartment of Physics and Astronomy, Uppsala University Box 516 SE-751 20 Uppsala Sweden carl.caleman@physics.uu.se.
Thomas MandlDepartment of Physics and Astronomy, Uppsala University Box 516 SE-751 20 Uppsala Sweden carl.caleman@physics.uu.se.
Christofer ÖstlinDepartment of Physics and Astronomy, Uppsala University Box 516 SE-751 20 Uppsala Sweden carl.caleman@physics.uu.se.ORCID https://orcid.org/0000-0002-0021-4354
Oscar GrånäsDepartment of Physics and Astronomy, Uppsala University Box 516 SE-751 20 Uppsala Sweden carl.caleman@physics.uu.se.ORCID https://orcid.org/0000-0002-1482-2182
Maxim N BrodmerkelDepartment of Chemistry - BMC, Uppsala University Box 576 SE-751 23 Uppsala Sweden erik.marklund@kemi.uu.se.ORCID https://orcid.org/0000-0003-0458-0623
Erik G MarklundDepartment of Chemistry - BMC, Uppsala University Box 576 SE-751 23 Uppsala Sweden erik.marklund@kemi.uu.se.ORCID https://orcid.org/0000-0002-9804-5009
Carl CalemanDepartment of Physics and Astronomy, Uppsala University Box 516 SE-751 20 Uppsala Sweden carl.caleman@physics.uu.se.ORCID https://orcid.org/0000-0003-2638-1940

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The dynamics of proteins are crucial for their function. However, commonly used techniques for studying protein structures are limited in monitoring time-resolved dynamics at high resolution. Combining electric fields with existing techniques to study gas-phase proteins, such as single particle imaging using free-electron lasers and gas-phase small angle X-ray scattering, has the potential to open up a new era in time-resolved studies of gas-phase protein dynamics. Using molecular dynamics simulations, we identify well-defined unfolding pathways of a protein, induced by experimentally achievable external electric fields. Our simulations show that strong electric fields in conjunction with short-pulsed X-ray sources such as free-electron lasers can be a new path for imaging dynamics of gas-phase proteins at high spatial and temporal resolution.

Identifiers

PMID34163965
PMCPMC8179335

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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.