Evidence map›Paper›PMID 36542701›Full record

ArticleScience advances2022

Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein.

Rajkamal Balu, Nisal Wanasingha, Jitendra P Mata, Agata Rekas, Susan Barrett, Geoff Dumsday, Aaron W Thornton, Anita J Hill, Namita Roy Choudhury, Naba K Dutta

Abstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. PEG-mCherry interactions beyond classical macromolecular crowding.Protein science : a publication of the Protein Society · 2025
    Article
  5. Review
  6. Article
  7. 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

10 authors.

Rajkamal BaluChemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia.ORCID 0000-0002-2748-8734
Nisal WanasinghaChemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia.ORCID 0000-0003-2709-8020
Jitendra P MataAustralian Center for Neutron Scattering, ANSTO, Lucas Heights, NSW 2234, Australia.ORCID 0000-0001-9225-7900
Agata RekasNational Deuteration Facility, ANSTO, Lucas Heights, NSW 2234, Australia.ORCID 0000-0003-2743-4506
Susan BarrettCSIRO Manufacturing, Bayview Avenue, Clayton, VIC 3168, Australia.ORCID 0000-0003-1132-5268
Geoff DumsdayCSIRO Manufacturing, Bayview Avenue, Clayton, VIC 3168, Australia.ORCID 0000-0002-5080-8791
Aaron W ThorntonCSIRO Manufacturing, Bayview Avenue, Clayton, VIC 3168, Australia.ORCID 0000-0002-7959-1397
Anita J HillCSIRO Manufacturing, Bayview Avenue, Clayton, VIC 3168, Australia.ORCID 0000-0003-1574-243X
Namita Roy ChoudhuryChemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia.ORCID 0000-0001-9010-8506
Naba K DuttaChemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia.ORCID 0000-0003-4800-1910

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The consequences of crowding on the dynamic conformational ensembles of intrinsically disordered proteins (IDPs) remain unresolved because of their ultrafast motion. Here, we report crowder-induced interactions and conformational dynamics of a prototypical multistimuli-responsive IDP, Rec1-resilin. The effects of a range of crowders of varying sizes, forms, topologies, and concentrations were examined using spectroscopic, spectrofluorimetric, and contrast-matching small- and ultrasmall-angle neutron scattering investigation. To achieve sufficient neutron contrast against the crowders, deuterium-labeled Rec1-resilin was biosynthesized successfully. Moreover, the ab initio "shape reconstruction" approach was used to obtain three-dimensional models of the conformational assemblies. The IDP revealed crowder-specific systematic extension and compaction with the level of macromolecular crowding. Last, a robust extension-contraction model has been postulated to capture the fundamental phenomena governing the observed behavior of IDPs. The study provides insights and fresh perspectives for understanding the interactions and structural dynamics of IDPs in crowded states.

Indexed as

Intrinsically Disordered ProteinsMacromolecular SubstancesProtein ConformationIntrinsically Disordered ProteinsMacromolecular Substances

Identifiers

PMID36542701
PMCPMC9770960

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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.