Evidence map›Paper›PMID 29058725›Full record

ArticleNature chemical biology2017

Rational design of proteins that exchange on functional timescales.

James A Davey, Adam M Damry, Natalie K Goto, Roberto A Chica

Abstract read
PubMed Publisher
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 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  3. Deep learning-guided design of dynamic proteins.Science (New York, N.Y.) · 2025
    Article
  4. Seesaw protein: Design of a protein that adopts interconvertible alternative functional conformations and its dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Exploiting conformational dynamics to modulate the function of designed proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  9. Article
  10. Article
  11. Reversible switching between two common protein folds in a designed system using only temperature.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Review
  13. Design and discovery of metamorphic proteins.Current opinion in structural biology · 2022
    Review
  14. Article
  15. Accurate positioning of functional residues with robotics-inspired computational protein design.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. The stability and dynamics of computationally designed proteins.Protein engineering, design & selection : PEDS · 2022
    Review
  18. Article
  19. Design principles of protein switches.Current opinion in structural biology · 2022
    Review
  20. Review
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

4 authors at 1 institution in 1 country.

James A DaveyDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada.
Adam M DamryDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada.
Natalie K GotoDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada.
Roberto A ChicaDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, Ottawa, Ontario, Canada.
University of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are intrinsically dynamic molecules that can exchange between multiple conformational states, enabling them to carry out complex molecular processes with extreme precision and efficiency. Attempts to design novel proteins with tailored functions have mostly failed to yield efficiencies matching those found in nature because standard methods do not allow the design of exchange between necessary conformational states on a functionally relevant timescale. Here we developed a broadly applicable computational method to engineer protein dynamics that we term meta-multistate design. We used this methodology to design spontaneous exchange between two novel conformations introduced into the global fold of Streptococcal protein G domain β1. The designed proteins, named DANCERs, for dynamic and native conformational exchangers, are stably folded and switch between predicted conformational states on the millisecond timescale. The successful introduction of defined dynamics on functional timescales opens the door to new applications requiring a protein to spontaneously access multiple conformational states.

Indexed as

Molecular Dynamics SimulationBacterial ProteinsProtein ConformationStreptococcusBacterial ProteinsIgG Fc-binding protein, Streptococcus

Identifiers

PMID29058725
OpenAlexW2952146947

What OpenQuestion holds

Textmetadata
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.