Evidence map›Paper›PMID 32502383›Full record

ArticleBiophysical journal2020

Distance-Based Metrics for Comparing Conformational Ensembles of Intrinsically Disordered Proteins.

Tamas Lazar, Mainak Guharoy, Wim Vranken, Sarah Rauscher, Shoshana J Wodak, Peter Tompa

Abstract read
In one paragraph

Article in Biophysical journal, 2020. 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
–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

15 citing papers in PubMed.

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  6. Protein ensemble modeling and analysis with MMMx.Protein science : a publication of the Protein Society · 2024
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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

6 authors.

Tamas LazarVIB-VUB Center for Structural Biology (CSB), Vlaams Instituut voor Biotechnologie, Brussels, Belgium; Structural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Mainak GuharoyVIB-VUB Center for Structural Biology (CSB), Vlaams Instituut voor Biotechnologie, Brussels, Belgium; Structural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium.
Wim VrankenStructural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium; Interuniversity Institute of Bioinformatics in Brussels, ULB-VUB, Brussels, Belgium.
Sarah RauscherDepartment of Physics & Department of Chemistry, University of Toronto, Toronto, Ontario, Canada; Department of Chemical and Physical Sciences, University of Toronto Mississauga, Mississauga, Ontario, Canada.
Shoshana J WodakVIB-VUB Center for Structural Biology (CSB), Vlaams Instituut voor Biotechnologie, Brussels, Belgium. Electronic address: shoshana.wodak@gmail.com.
Peter TompaVIB-VUB Center for Structural Biology (CSB), Vlaams Instituut voor Biotechnologie, Brussels, Belgium; Structural Biology Brussels (SBB), Vrije Universiteit Brussel (VUB), Brussels, Belgium; Institute of Enzymology, Research Centre for Natural Sciences of the Hungarian Academy of Sciences, Budapest, Hungary. Electronic address: peter.tompa@vub.be.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intrinsically disordered proteins are proteins whose native functional states represent ensembles of highly diverse conformations. Such ensembles are a challenge for quantitative structure comparisons because their conformational diversity precludes optimal superimposition of the atomic coordinates necessary for deriving common similarity measures such as the root mean-square deviation of these coordinates. Here, we introduce superimposition-free metrics that are based on computing matrices of the Cα-Cα distance distributions within ensembles and comparing these matrices between ensembles. Differences between two matrices yield information on the similarity between specific regions of the polypeptide, whereas the global structural similarity is captured by the root mean-square difference between the medians of the Cα-Cα distance distributions of two ensembles. Together, our metrics enable rigorous investigations of structure-function relationships in conformational ensembles of intrinsically disordered proteins derived using experimental restraints or by molecular simulations and for proteins containing both structured and disordered regions.

Indexed as

Intrinsically Disordered ProteinsPeptidesProtein ConformationIntrinsically Disordered ProteinsPeptides

Identifiers

PMID32502383
PMCPMC7300341

What OpenQuestion holds

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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.