Evidence map›Paper›PMID 38177681›Full record

ArticleNature structural & molecular biology2024

Design of complicated all-α protein structures.

Koya Sakuma, Naohiro Kobayashi, Toshihiko Sugiki, Toshio Nagashima, Toshimichi Fujiwara, Kano Suzuki, Naoya Kobayashi, Takeshi Murata, Takahiro Kosugi, Rie Tatsumi-Koga and 1 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Rapidly evolving aphid gall effector proteins exhibit saposin-like folds.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Limitations of the refolding pipeline for de novo protein design.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Rapidly evolving aphid gall effector proteins exhibit saposin-like folds.bioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  7. Article
  8. Article
  9. Article
  10. Protein Structure Inspired Drug Discovery.bioRxiv : the preprint server for biology · 2024
    Article
  11. State-Targeting Stabilization of Adenosine AInternational journal of molecular sciences · 2021
    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

11 authors.

Koya Sakuma *Department of Structural Molecular Science, School of Physical Sciences, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Japan.ORCID http://orcid.org/0000-0003-2083-0979
Naohiro Kobayashi *RIKEN Center for Biosystems Dynamics Research, RIKEN, Yokohama, Japan.
Toshihiko SugikiInstitute for Protein Research, Osaka University, Suita, Japan.ORCID http://orcid.org/0000-0003-1716-1241
Toshio NagashimaRIKEN Center for Biosystems Dynamics Research, RIKEN, Yokohama, Japan.
Toshimichi FujiwaraInstitute for Protein Research, Osaka University, Suita, Japan.ORCID http://orcid.org/0000-0001-7739-3525
Kano SuzukiDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.ORCID http://orcid.org/0000-0001-9467-9728
Naoya KobayashiProtein Design Group, Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of National Sciences, Okazaki, Japan.ORCID http://orcid.org/0000-0002-6599-1680
Takeshi MurataDepartment of Chemistry, Graduate School of Science, Chiba University, Chiba, Japan.ORCID http://orcid.org/0000-0002-5748-4670
Takahiro KosugiDepartment of Structural Molecular Science, School of Physical Sciences, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Japan.ORCID http://orcid.org/0000-0002-6289-5319
Rie Tatsumi-KogaProtein Design Group, Exploratory Research Center on Life and Living Systems (ExCELLS), National Institutes of National Sciences, Okazaki, Japan.ORCID http://orcid.org/0000-0002-5068-1049
Nobuyasu KogaDepartment of Structural Molecular Science, School of Physical Sciences, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Japan. nkoga@protein.osaka-u.ac.jp.ORCID http://orcid.org/0000-0001-8457-0809

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A wide range of de novo protein structure designs have been achieved, but the complexity of naturally occurring protein structures is still far beyond these designs. Here, to expand the diversity and complexity of de novo designed protein structures, we sought to develop a method for designing 'difficult-to-describe' α-helical protein structures composed of irregularly aligned α-helices like globins. Backbone structure libraries consisting of a myriad of α-helical structures with five or six helices were generated by combining 18 helix-loop-helix motifs and canonical α-helices, and five distinct topologies were selected for de novo design. The designs were found to be monomeric with high thermal stability in solution and fold into the target topologies with atomic accuracy. This study demonstrated that complicated α-helical proteins are created using typical building blocks. The method we developed will enable us to explore the universe of protein structures for designing novel functional proteins.

Indexed as

Protein FoldingProteinsProtein Conformation, alpha-HelicalProtein Structure, SecondaryProteins

Identifiers

PMID38177681
PMCPMC11377298

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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.