Evidence map›Paper›PMID 39196930›Full record

ArticleScience advances2024

Design of intrinsically disordered protein variants with diverse structural properties.

Francesco Pesce, Anne Bremer, Giulio Tesei, Jesse B Hopkins, Christy R Grace, Tanja Mittag, Kresten Lindorff-Larsen

Abstract read
In one paragraph

Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
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  8. Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026
    Article
  9. Article
  10. Intrinsic Disorder as a Biomimetic Design Paradigm.Biomimetics (Basel, Switzerland) · 2026
    Article
  11. Generative design of intrinsically disordered protein regions with IDiom.bioRxiv : the preprint server for biology · 2026
    Article
  12. Article
  13. Review
  14. Novel Prion Protein Gene (bioRxiv : the preprint server for biology · 2026
    Article
  15. Review
  16. Article
  17. Article
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  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Francesco PesceStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-3403-2524
Anne BremerDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.ORCID 0000-0002-2525-1813
Giulio TeseiStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0003-4339-4460
Jesse B HopkinsBioCAT, Department of Physics, Illinois Institute of Technology, Chicago, IL 60616, USA.ORCID 0000-0001-8554-8072
Christy R GraceDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.ORCID 0000-0002-1600-5610
Tanja MittagDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.ORCID 0000-0002-1827-3811
Kresten Lindorff-LarsenStructural Biology and NMR Laboratory, The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-4750-6039

Funding

The Biophysics Collaborative Access Team (User Training and Outreach)P30GM138395 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI THOMAS C IRVING · 2021 to 2026
$16.5M
Understanding the Sequence and Structural Determinants of Phase Behavior of ALS-Causing ProteinsR01NS121114 · NINDS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI Tanja Mittag, ROHIT V PAPPU · 2021 to 2026
$3.8M
NIGMS NIH HHS P30 GM138395NINDS NIH HHS R01 NS121114
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) perform a broad range of functions in biology, suggesting that the ability to design IDPs could help expand the repertoire of proteins with novel functions. Computational design of IDPs with specific conformational properties has, however, been difficult because of their substantial dynamics and structural complexity. We describe a general algorithm for designing IDPs with specific structural properties. We demonstrate the power of the algorithm by generating variants of naturally occurring IDPs that differ in compaction, long-range contacts, and propensity to phase separate. We experimentally tested and validated our designs and analyzed the sequence features that determine conformations. We show how our results are captured by a machine learning model, enabling us to speed up the algorithm. Our work expands the toolbox for computational protein design and will facilitate the design of proteins whose functions exploit the many properties afforded by protein disorder.

Indexed as

AlgorithmsIntrinsically Disordered ProteinsProtein ConformationComputational BiologyMachine LearningModels, MolecularProtein EngineeringIntrinsically Disordered Proteins

Identifiers

PMID39196930
PMCPMC11352843

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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.