Evidence map›Paper›PMID 35132077›Full record

ArticleScientific reports2022

Modelling of the dynamic polarizability of macromolecules for single-molecule optical biosensing.

Larnii S Booth, Eloise V Browne, Nicolas P Mauranyapin, Lars S Madsen, Shelley Barfoot, Alan Mark, Warwick P Bowen

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

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  15. Optical Monitoring ofNano letters · 2023
    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 at 1 institution in 1 country.

Larnii S BoothARC Centre for Engineered Quantum Systems (EQUS), School of Mathematics and Physics, The University of Queensland, Brisbane, Australia.
Eloise V BrowneARC Centre for Engineered Quantum Systems (EQUS), School of Mathematics and Physics, The University of Queensland, Brisbane, Australia.
Nicolas P MauranyapinARC Centre for Engineered Quantum Systems (EQUS), School of Mathematics and Physics, The University of Queensland, Brisbane, Australia.
Lars S MadsenARC Centre for Engineered Quantum Systems (EQUS), School of Mathematics and Physics, The University of Queensland, Brisbane, Australia.
Shelley BarfootSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Australia.
Alan MarkSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Australia.
Warwick P BowenARC Centre for Engineered Quantum Systems (EQUS), School of Mathematics and Physics, The University of Queensland, Brisbane, Australia. w.bowen@uq.edu.au.
University of Queensland · AU

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
NIGMS NIH HHS P41 GM103311
6 · The paper itself

Abstract

The structural dynamics of macromolecules is important for most microbiological processes, from protein folding to the origins of neurodegenerative disorders. Noninvasive measurements of these dynamics are highly challenging. Recently, optical sensors have been shown to allow noninvasive time-resolved measurements of the dynamic polarizability of single-molecules. Here we introduce a method to efficiently predict the dynamic polarizability from the atomic configuration of a given macromolecule. This provides a means to connect the measured dynamic polarizability to the underlying structure of the molecule, and therefore to connect temporal measurements to structural dynamics. To illustrate the methodology we calculate the change in polarizability as a function of time based on conformations extracted from molecular dynamics simulations and using different conformations of motor proteins solved crystalographically. This allows us to quantify the magnitude of the changes in polarizablity due to thermal and functional motions.

Indexed as

Molecular Dynamics SimulationBiosensing TechniquesMacromolecular SubstancesProtein FoldingProteinsMacromolecular SubstancesProteins

Identifiers

PMID35132077
PMCPMC8821610
OpenAlexW4210905162

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.