Evidence map›Paper›PMID 26042819›Full record

ArticleScientific reports2015

Structural ensembles reveal intrinsic disorder for the multi-stimuli responsive bio-mimetic protein Rec1-resilin.

Rajkamal Balu, Robert Knott, Nathan P Cowieson, Christopher M Elvin, Anita J Hill, Namita R Choudhury, Naba K Dutta

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 41 citations in OpenAlex.

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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

7 authors at 5 institutions in 1 country.

Rajkamal BaluIan Wark Research Institute, University of South Australia, Mawson Lakes campus, Mawson lakes, South Australia 5095, Australia.
Robert KnottANSTO, Private Mail Bag, Kirrawee, New South Wales 2232, Australia.
Nathan P CowiesonCentre for Synchrotron Science, Monash University, Victoria 3800, Australia.
Christopher M ElvinCSIRO Agriculture, Level 6, Queensland Bioscience Precinct, St Lucia, Queensland 4067, Australia.
Anita J HillCSIRO Manufacturing, Clayton, Victoria 3168, Australia.
Namita R ChoudhuryIan Wark Research Institute, University of South Australia, Mawson Lakes campus, Mawson lakes, South Australia 5095, Australia.
Naba K DuttaIan Wark Research Institute, University of South Australia, Mawson Lakes campus, Mawson lakes, South Australia 5095, Australia.
University of South Australia · AUAustralian Nuclear Science and Technology Organisation · AUCommonwealth Scientific and Industrial Research Organisation · AUCSIRO Manufacturing · AUMonash University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rec1-resilin is the first recombinant resilin-mimetic protein polymer, synthesized from exon-1 of the Drosophila melanogaster gene CG15920 that has demonstrated unusual multi-stimuli responsiveness in aqueous solution. Crosslinked hydrogels of Rec1-resilin have also displayed remarkable mechanical properties including near-perfect rubber-like elasticity. The structural basis of these extraordinary properties is not clearly understood. Here we combine a computational and experimental investigation to examine structural ensembles of Rec1-resilin in aqueous solution. The structure of Rec1-resilin in aqueous solutions is investigated experimentally using circular dichroism (CD) spectroscopy and small angle X-ray scattering (SAXS). Both bench-top and synchrotron SAXS are employed to extract structural data sets of Rec1-resilin and to confirm their validity. Computational approaches have been applied to these experimental data sets in order to extract quantitative information about structural ensembles including radius of gyration, pair-distance distribution function, and the fractal dimension. The present work confirms that Rec1-resilin is an intrinsically disordered protein (IDP) that displays equilibrium structural qualities between those of a structured globular protein and a denatured protein. The ensemble optimization method (EOM) analysis reveals a single conformational population with partial compactness. This work provides new insight into the structural ensembles of Rec1-resilin in solution.

Indexed as

Protein ConformationCircular DichroismInsect ProteinsProtein Structure, SecondaryScattering, Small AngleX-Ray DiffractionInsect Proteinsresilin

Identifiers

PMID26042819
PMCPMC4455251
OpenAlexW2342614422

What OpenQuestion holds

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LicenceCC BY
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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.