Evidence map›Paper›PMID 31667345›Full record

ArticleScience advances2019

Intrinsically disordered proteins access a range of hysteretic phase separation behaviors.

Felipe Garcia Quiroz, Nan K Li, Stefan Roberts, Patrick Weber, Michael Dzuricky, Isaac Weitzhandler, Yaroslava G Yingling, Ashutosh Chilkoti

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
  2. Chemical reviews · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Non-Fickian diffusion within assemblies of the intrinsically disordered protein β-casein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Review
  9. A Novel Gene Synthesis Platform for Designing Functional Protein Polymers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
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  19. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Felipe Garcia QuirozDepartment of Biomedical Engineering, Duke University, Durham, NC 27708, USA.ORCID 0000-0001-6454-9615
Nan K LiDepartment of Materials Science and Engineering, North Carolina State University, 911 Partners Way, Raleigh, NC 27695, USA.ORCID 0000-0001-7340-6958
Stefan RobertsDepartment of Biomedical Engineering, Duke University, Durham, NC 27708, USA.ORCID 0000-0001-7393-8049
Patrick WeberSwiss Nanoscience Institute, University of Basel, Klingelbergstrasse 82, 4056 Basel, Switzerland.
Michael DzurickyDepartment of Biomedical Engineering, Duke University, Durham, NC 27708, USA.ORCID 0000-0002-1775-2132
Isaac WeitzhandlerDepartment of Biomedical Engineering, Duke University, Durham, NC 27708, USA.
Yaroslava G YinglingDepartment of Materials Science and Engineering, North Carolina State University, 911 Partners Way, Raleigh, NC 27695, USA.ORCID 0000-0002-8557-9992
Ashutosh ChilkotiDepartment of Biomedical Engineering, Duke University, Durham, NC 27708, USA.ORCID 0000-0002-1569-2228
Duke University · USNorth Carolina State University · USUniversity of Basel · CH

Funding

ELASTIN FUSION PROTEINSR01GM061232 · NIGMS · DUKE UNIVERSITY · PI CHILKOTI, ASHUTOSH · 2000 to 2017
$4.6M
Genetically Encoded Smart Biohybrid MaterialsR35GM127042 · NIGMS · DUKE UNIVERSITY · PI CHILKOTI, ASHUTOSH · 2018 to 2022
$2.2M
NIGMS NIH HHS R01 GM061232NIGMS NIH HHS R35 GM127042
6 · The paper itself

Abstract

The phase separation behavior of intrinsically disordered proteins (IDPs) is thought of as analogous to that of polymers that undergo equilibrium lower or upper critical solution temperature (LCST and UCST, respectively) phase transition. This view, however, ignores possible nonequilibrium properties of protein assemblies. Here, by studying IDP polymers (IDPPs) composed of repeat motifs that encode LCST or UCST phase behavior, we discovered that IDPs can access a wide spectrum of nonequilibrium, hysteretic phase behaviors. Experimentally and through simulations, we show that hysteresis in IDPPs is tunable and that it emerges through increasingly stable interchain interactions in the insoluble phase. To explore the utility of hysteretic IDPPs, we engineer self-assembling nanostructures with tunable stability. These findings shine light on the rich phase separation behavior of IDPs and illustrate hysteresis as a design parameter to program nonequilibrium phase behavior in self-assembling materials.

Indexed as

Amino AcidsAntifreeze ProteinsCircular DichroismHydrogen BondingHydrophobic and Hydrophilic InteractionsIntrinsically Disordered ProteinsMolecular Dynamics SimulationNanoparticlesPhase TransitionProlineTemperatureUreaAmino AcidsAntifreeze ProteinsIntrinsically Disordered ProteinsProlineUrea

Identifiers

PMID31667345
PMCPMC6799979
OpenAlexW2980586256

What OpenQuestion holds

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Registered trials

None linked

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.