Evidence map›Paper›PMID 30433771›Full record

ArticleJournal of the American Chemical Society2018

Enhancing Protein Stability with Genetically Encoded Noncanonical Amino Acids.

Jack C Li, Tao Liu, Yan Wang, Angad P Mehta, Peter G Schultz

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Multicyclic D-Stereospecific Hydrolase Dimer With High Sustained Activity.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Catalytic pBiochemistry · 2026
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Recent advances in the expanding genetic code.Current opinion in chemical biology · 2024
    Review
  15. Review
  16. Review
  17. Review
  18. Review
  19. Synthesis at the Interface of Chemistry and Biology.Accounts of chemical research · 2024
    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

5 authors.

Jack C LiDepartment of Chemistry and Skaggs Institute for Chemical Biology , The Scripps Research Institute , La Jolla , California 92037 , United States.
Tao LiuDepartment of Chemistry and Skaggs Institute for Chemical Biology , The Scripps Research Institute , La Jolla , California 92037 , United States.ORCID 0000-0001-5347-5892
Yan WangDepartment of Chemistry and Skaggs Institute for Chemical Biology , The Scripps Research Institute , La Jolla , California 92037 , United States.
Angad P MehtaDepartment of Chemistry and Skaggs Institute for Chemical Biology , The Scripps Research Institute , La Jolla , California 92037 , United States.
Peter G SchultzDepartment of Chemistry and Skaggs Institute for Chemical Biology , The Scripps Research Institute , La Jolla , California 92037 , United States.ORCID 0000-0003-3188-1202

Funding

IN VIVO INCORPORATION OF UNNATURAL AMINO ACIDSR01GM062159 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHULTZ, PETER G · 2001 to 2022
$8.2M
NIGMS NIH HHS R01 GM062159
6 · The paper itself

Abstract

The ability to add noncanonical amino acids to the genetic code may allow one to evolve proteins with new or enhanced properties using a larger set of building blocks. To this end, we have been able to select mutant proteins with enhanced thermal properties from a library of E. coli homoserine O-succinyltransferase ( metA) mutants containing randomly incorporated noncanonical amino acids. Here, we show that substitution of Phe 21 with ( p-benzoylphenyl)alanine (pBzF), increases the melting temperature of E. coli metA by 21 °C. This dramatic increase in thermal stability, arising from a single mutation, likely results from a covalent adduct between Cys 90 and the keto group of pBzF that stabilizes the dimeric form of the enzyme. These experiments show that an expanded genetic code can provide unique solutions to the evolution of proteins with enhanced properties.

Indexed as

BenzophenonesEscherichia coliEscherichia coli ProteinsHomoserine O-SuccinyltransferaseMutationPhenylalanineProtein DomainsProtein EngineeringProtein StabilityTemperature4-benzoylphenylalanineBenzophenonesEscherichia coli ProteinsHomoserine O-SuccinyltransferasemetA protein, E coliPhenylalanine

Identifiers

PMID30433771
PMCPMC6426444

What OpenQuestion holds

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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.