Evidence map›Paper›PMID 38429263›Full record

ArticleNature communications2024

Sequence-dependent material properties of biomolecular condensates and their relation to dilute phase conformations.

Dinesh Sundaravadivelu Devarajan, Jiahui Wang, Beata Szała-Mendyk, Shiv Rekhi, Arash Nikoubashman, Young C Kim, Jeetain Mittal

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

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  17. Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  18. Review
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3 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Dinesh Sundaravadivelu DevarajanArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843, USA. dineshsd@tamu.edu.ORCID 0000-0001-7825-0999
Jiahui WangArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843, USA.
Beata Szała-MendykArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843, USA.ORCID 0000-0001-7858-7444
Shiv RekhiArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843, USA.
Arash NikoubashmanLeibniz-Institut für Polymerforschung Dresden e.V., Hohe Straße 6, 01069, Dresden, Germany.ORCID 0000-0003-0563-825X
Young C KimCenter for Materials Physics and Technology, Naval Research Laboratory, Washington, DC, 20375, USA.
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, 77843, USA. jeetain@tamu.edu.ORCID 0000-0002-9725-6402

Funding

Liquid-Liquid Phase Separation in Heterochromatin OrganizationR01GM136917 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI MITTAL, JEETAIN · 2020 to 2023
$1.4M
Multiscale Computational Models to Investigate the Role of Phase Separation in BiologyR35GM153388 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI Jeetain Mittal · 2024 to 2026
$1.3M
NIGMS NIH HHS R01 GM136917NIGMS NIH HHS R35 GM153388
6 · The paper itself

Abstract

Material properties of phase-separated biomolecular condensates, enriched with disordered proteins, dictate many cellular functions. Contrary to the progress made in understanding the sequence-dependent phase separation of proteins, little is known about the sequence determinants of condensate material properties. Using the hydropathy scale and Martini models, we computationally decipher these relationships for charge-rich disordered protein condensates. Our computations yield dynamical, rheological, and interfacial properties of condensates that are quantitatively comparable with experimentally characterized condensates. Interestingly, we find that the material properties of model and natural proteins respond similarly to charge segregation, despite different sequence compositions. Molecular interactions within the condensates closely resemble those within the single-chain ensembles. Consequently, the material properties strongly correlate with molecular contact dynamics and single-chain structural properties. We demonstrate the potential to harness the sequence characteristics of disordered proteins for predicting and engineering the material properties of functional condensates, with insights from the dilute phase properties.

Indexed as

Biomolecular CondensatesEngineeringMolecular ConformationPhase SeparationRheology

Identifiers

PMID38429263
PMCPMC10907393

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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.