Evidence map›Paper›PMID 28572639›Full record

ArticleScientific reports2017

Construction of novel repeat proteins with rigid and predictable structures using a shared helix method.

Suk-Jun Youn, Na-Young Kwon, Ji Hyun Lee, Jin Hong Kim, Jinwoo Choi, Hayyoung Lee, Jie-Oh Lee

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Article
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  10. Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies).Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
  12. Allosteric cooperation in a de novo-designed two-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Modular repeat protein sculpting using rigid helical junctions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Development of imaging scaffolds for cryo-electron microscopy.Current opinion in structural biology · 2020
    Review
  16. 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

7 authors.

Suk-Jun YounDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Korea.
Na-Young KwonDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Korea.
Ji Hyun LeeDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Korea.
Jin Hong KimDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Korea.
Jinwoo ChoiDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Korea.
Hayyoung LeeInstitute of Biotechnology, Chungnam National University, Daejeon, Korea.
Jie-Oh LeeDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 34141, Korea. jieoh@kaist.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Generating artificial protein assemblies with complex shapes requires a method for connecting protein components with stable and predictable structures. Currently available methods for creating rigid protein assemblies rely on either complicated calculations or extensive trial and error. We describe a simple and efficient method for connecting two proteins via a fused alpha helix that is formed by joining two preexisting helices into a single extended helix. Because the end-to-end ligation of helices does not guarantee the formation of a continuous helix, we superimposed 1-2 turns of pairs of connecting helices by using a molecular graphics program. Then, we chose amino acids from the two natural sequences that would stabilize the connecting helix. This "shared helix method" is highly efficient. All the designed proteins that could be produced in Escherichia coli were readily crystallized and had the expected fusion structures. To prove the usefulness of this method, we produced two novel repeat proteins by assembling several copies of natural or artificial proteins with alpha helices at both termini. Their crystal structures demonstrated the successful assembly of the repeating units with the intended curved shapes. We propose that this method could dramatically expand the available repertoire of natural repeat proteins.

Indexed as

Amino AcidsCrystallography, X-RayEscherichia coliGene ExpressionGenetic EngineeringHumansHydrogen BondingModels, MolecularProtein Conformation, alpha-HelicalRecombinant Fusion ProteinsAmino AcidsRecombinant Fusion Proteins

Identifiers

PMID28572639
PMCPMC5454011

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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.