Evidence map›Paper›PMID 28530710›Full record

ArticleNature chemical biology2017

Engineering protein stability with atomic precision in a monomeric miniprotein.

Emily G Baker, Christopher Williams, Kieran L Hudson, Gail J Bartlett, Jack W Heal, Kathryn L Porter Goff, Richard B Sessions, Matthew P Crump, Derek N Woolfson

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 57 citations in OpenAlex.

  1. The Ascent of Miniproteins.Biochemistry · 2026
    Review
  2. Article
  3. Journal of chemical information and modeling · 2025
    Article
  4. Chemical science · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. The Energetic Origins of Pi-Pi Contacts in Proteins.Journal of the American Chemical Society · 2023
    Article
  9. AQcalc: A web server that identifies weak molecular interactions in protein structures.Protein science : a publication of the Protein Society · 2023
    Article
  10. Review
  11. Article
  12. Dissecting the stability determinants of a challenging de novo protein fold using massively parallel design and experimentation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Secondary Forces in Protein Folding.ACS chemical biology · 2019
    Review
  20. 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

9 authors at 1 institution in 1 country.

Emily G BakerSchool of Chemistry, University of Bristol, Bristol, UK.ORCID http://orcid.org/0000-0002-1593-5525
Christopher WilliamsSchool of Chemistry, University of Bristol, Bristol, UK.ORCID http://orcid.org/0000-0001-5806-9842
Kieran L HudsonSchool of Chemistry, University of Bristol, Bristol, UK.ORCID http://orcid.org/0000-0002-3566-7003
Gail J BartlettSchool of Chemistry, University of Bristol, Bristol, UK.
Jack W HealSchool of Chemistry, University of Bristol, Bristol, UK.
Kathryn L Porter GoffSchool of Chemistry, University of Bristol, Bristol, UK.
Richard B SessionsBrisSynBio, University of Bristol, Bristol, UK.
Matthew P CrumpSchool of Chemistry, University of Bristol, Bristol, UK.ORCID http://orcid.org/0000-0002-7868-5818
Derek N WoolfsonSchool of Chemistry, University of Bristol, Bristol, UK.ORCID http://orcid.org/0000-0002-0394-3202
University of Bristol · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/M005615/1European Research Council 340764Wellcome Trust 082352Wellcome Trust 099185
6 · The paper itself

Abstract

Miniproteins simplify the protein-folding problem, allowing the dissection of forces that stabilize protein structures. Here we describe PPα-Tyr, a designed peptide comprising an α-helix buttressed by a polyproline II helix. PPα-Tyr is water soluble and monomeric, and it unfolds cooperatively with a midpoint unfolding temperature (T

Indexed as

PeptidesProtein EngineeringProtein FoldingProtein StabilityTemperaturePeptides

Identifiers

PMID28530710
PMCPMC5860740
OpenAlexW2617643277

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.