Evidence map›Paper›PMID 33602829›Full record

ArticleScience (New York, N.Y.)2021

De novo design of transmembrane β barrels.

Anastassia A Vorobieva, Paul White, Binyong Liang, Jim E Horne, Asim K Bera, Cameron M Chow, Stacey Gerben, Sinduja Marx, Alex Kang, Alyssa Q Stiving and 9 more

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing 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

73 citing papers in PubMed.

  1. Article
  2. Sculpting semisynthetic conducting protein pores by de novo design.Nature structural & molecular biology · 2026
    Article
  3. Generative design of programmable asymmetric β-barrel nanopores.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Review
  6. Limitations of the refolding pipeline for de novo protein design.Protein science : a publication of the Protein Society · 2026
    Article
  7. Article
  8. Negative design enables cell-free expression and folding of designed transmembrane β-barrels.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  9. Review
  10. Article
  11. Review
  12. β-barrels from short macrocyclic peptides.Chemical communications (Cambridge, England) · 2026
    Article
  13. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Parametrically guided design of beta barrels and transmembrane nanopores using deep learning.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article

13 more citing papers are in PubMed but not listed here.

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

19 authors.

Anastassia A VorobievaDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID https://orcid.org/0000-0001-5554-1398
Paul White *Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.ORCID https://orcid.org/0000-0001-7536-4552
Binyong Liang *Department of Molecular Physiology and Biological Physics and Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA 22903, USA.ORCID https://orcid.org/0000-0001-9347-4958
Jim E HorneAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.ORCID https://orcid.org/0000-0001-5260-2634
Asim K BeraDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Cameron M ChowDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID https://orcid.org/0000-0001-5351-6412
Stacey GerbenDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID https://orcid.org/0000-0003-0313-6248
Sinduja MarxDepartment of Molecular Engineering and Sciences, University of Washington, Seattle, WA 98195, USA.ORCID https://orcid.org/0000-0002-6126-6019
Alex KangDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID https://orcid.org/0000-0001-5487-0499
Alyssa Q StivingDepartment of Chemistry and Biochemistry, Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.
Sophie R HarveyDepartment of Chemistry and Biochemistry, Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.ORCID https://orcid.org/0000-0003-0763-8173
Dagan C MarxTC Jenkins Department of Biophysics Johns Hopkins University, Baltimore, MD 21218, USA.ORCID https://orcid.org/0000-0003-0149-3778
G Nasir KhanAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.ORCID https://orcid.org/0000-0002-1834-2485
Karen G FlemingTC Jenkins Department of Biophysics Johns Hopkins University, Baltimore, MD 21218, USA.ORCID https://orcid.org/0000-0001-5417-8830
Vicki H WysockiDepartment of Chemistry and Biochemistry, Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, OH 43210, USA.ORCID https://orcid.org/0000-0003-0495-2538
David J BrockwellAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.ORCID https://orcid.org/0000-0002-0802-5937
Lukas K TammDepartment of Molecular Physiology and Biological Physics and Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, VA 22903, USA.ORCID https://orcid.org/0000-0002-1674-4464
Sheena E RadfordAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, USA.ORCID https://orcid.org/0000-0002-3079-8039
David BakerDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA. dabaker@uw.edu.ORCID https://orcid.org/0000-0001-7896-6217

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI Nozomi Ando, J Christopher Fromme · 2018 to 2026
$34.2M
Structural Dynamics of the Exocytotic Fusion Machine in Neurons.P01GM072694 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI KIESSLING, VOLKER · 2005 to 2021
$17.4M
PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI WYSOCKI, VICKI H. · 2018 to 2022
$7.6M
Structure, Assembly, and Function of Outer Membrane ProteinsR01GM051329 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI TAMM, LUKAS K · 1997 to 2018
$6.4M
Membrane Protein StabilityR01GM079440 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI FLEMING, KAREN G. · 2009 to 2022
$4.1M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Howard Hughes Medical InstituteMedical Research Council MR/P018491/1NIGMS NIH HHS P01 GM072694NIGMS NIH HHS P30 GM124165NIGMS NIH HHS P41 GM128577NIGMS NIH HHS R01 GM051329NIGMS NIH HHS R01 GM079440NIGMS NIH HHS T32 GM008403NIH HHS S10 OD021527Wellcome Trust
6 · The paper itself

Abstract

Transmembrane β-barrel proteins (TMBs) are of great interest for single-molecule analytical technologies because they can spontaneously fold and insert into membranes and form stable pores, but the range of pore properties that can be achieved by repurposing natural TMBs is limited. We leverage the power of de novo computational design coupled with a "hypothesis, design, and test" approach to determine TMB design principles, notably, the importance of negative design to slow β-sheet assembly. We design new eight-stranded TMBs, with no homology to known TMBs, that insert and fold reversibly into synthetic lipid membranes and have nuclear magnetic resonance and x-ray crystal structures very similar to the computational models. These advances should enable the custom design of pores for a wide range of applications.

Indexed as

Computer SimulationModels, MolecularProtein Conformation, beta-StrandProtein EngineeringAmino Acid SequenceCrystallography, X-RayHydrogen BondingHydrophobic and Hydrophilic InteractionsLipid BilayersMagnetic Resonance SpectroscopyMembrane ProteinsMembranes, ArtificialMicellesProtein ConformationProtein FoldingProtein StabilityLipid BilayersMembrane ProteinsMembranes, ArtificialMicelles

Identifiers

PMID33602829
PMCPMC8064278

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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.