Evidence map›Paper›PMID 32357776›Full record

ArticleThe Journal of chemical physics2020

An analytical theory to describe sequence-specific inter-residue distance profiles for polyampholytes and intrinsically disordered proteins.

Jonathan Huihui, Kingshuk Ghosh

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. A Sequence-Specific Theory for Charge-Regulating IDPs.The journal of physical chemistry. B · 2026
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  6. HYPK: A marginally disordered protein sensitive to charge decoration.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  7. Review
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  9. 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

2 authors.

Jonathan HuihuiDepartment of Physics and Astronomy, University of Denver, Denver, Colorado 80208, USA and Molecular and Cellular Biophysics, University of Denver, Denver, Colorado 80208, USA.ORCID 0000000231202823
Kingshuk GhoshDepartment of Physics and Astronomy, University of Denver, Denver, Colorado 80208, USA and Molecular and Cellular Biophysics, University of Denver, Denver, Colorado 80208, USA.ORCID 0000000349760986

Funding

Quantifying fluctuations to buildpredictive models and guide design of gene networksR15GM128162 · NIGMS · UNIVERSITY OF DENVER (COLORADO SEMINARY) · PI GHOSH, KINGSHUK · 2018 to 2018
$367k
NIGMS NIH HHS R15 GM128162
6 · The paper itself

Abstract

Intrinsically Disordered Proteins (IDPs), unlike folded proteins, lack a unique folded structure and rapidly interconvert among ensembles of disordered states. However, they have specific conformational properties when averaged over their ensembles of disordered states. It is critical to develop a theoretical formalism to predict these ensemble average conformational properties that are encoded in the IDP sequence (the specific order in which amino acids/residues are linked). We present a general heteropolymer theory that analytically computes the ensemble average distance profiles (⟨R

Indexed as

Molecular Dynamics SimulationAmino AcidsIntrinsically Disordered ProteinsMonte Carlo MethodPolymersProtein ConformationProtein FoldingStatic ElectricityAmino AcidsIntrinsically Disordered ProteinsPolymers

Identifiers

PMID32357776
PMCPMC7180065

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.