Evidence map›Paper›PMID 31181898›Full record

ArticleACS chemical biology2019

A Single Reactive Noncanonical Amino Acid Is Able to Dramatically Stabilize Protein Structure.

Jack C Li, Fariborz Nastertorabi, Weimin Xuan, Gye Won Han, Raymond C Stevens, Peter G Schultz

Erratum issuedAbstract read
In one paragraph

Article in ACS chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 29 citations in OpenAlex.

  1. In Vivo Biosynthesis and Direct Incorporation of Noncanonical Amino Acids into Proteins.Chembiochem : a European journal of chemical biology · 2025
    Review
  2. Article
  3. Recent advances in the expanding genetic code.Current opinion in chemical biology · 2024
    Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Non-canonical amino acids as a tool for the thermal stabilization of enzymes.Protein engineering, design & selection : PEDS · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Jack C LiDepartment of Chemistry and Skaggs Institute for Chemical Biology , The Scripps Research Institute , La Jolla , California 92037 , United States.
Fariborz NastertorabiDepartment of Biological Sciences, Bridge Institute, Michaelson Center for Convergent Bioscience , University of Southern California , Los Angeles , California 90089 , United States.
Weimin XuanDepartment of Chemistry and Skaggs Institute for Chemical Biology , The Scripps Research Institute , La Jolla , California 92037 , United States.
Gye Won HanDepartment of Biological Sciences, Bridge Institute, Michaelson Center for Convergent Bioscience , University of Southern California , Los Angeles , California 90089 , United States.
Raymond C StevensDepartment of Biological Sciences, Bridge Institute, Michaelson Center for Convergent Bioscience , University of Southern California , Los Angeles , California 90089 , 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
Scripps Research Institute · USUniversity of Southern California · US

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

A p-isothiocyanate phenylalanine mutant of the homodimeric protein homoserine o-succinyltransferase (MetA) was isolated in a temperature dependent selection from a library of metA mutants containing noncanonical amino acids. This mutant protein has a dramatic increase of 24 °C in thermal stability compared to the wild type protein. Peptide mapping experiments revealed that the isothiocyanate group forms a thiourea cross-link to the N terminal proline of the other monomer, despite the two positions being >30 Å apart in the X-ray crystal structure of the wild type protein. These results show that an expanded set of building blocks beyond the canonical 20 amino acids can lead to significant changes in the properties of proteins.

Indexed as

Crystallography, X-RayEscherichia coliEscherichia coli ProteinsHomoserine O-SuccinyltransferaseMutationPhenylalanineProtein ConformationProtein StabilityTemperatureEscherichia coli ProteinsHomoserine O-SuccinyltransferasePhenylalanine

Identifiers

PMID31181898
PMCPMC6791372
OpenAlexW4252171385

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.