Evidence map›Paper›PMID 26034281›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

tRNA acceptor stem and anticodon bases form independent codes related to protein folding.

Charles W Carter, Richard Wolfenden

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
5.0field-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

35 citing papers in PubMed, 82 citations in OpenAlex.

  1. Emergence of biosignatures on Earth and implications for life detection.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. The central dogma in reverse.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Science of the gaps.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
    Article
  4. Article
  5. Review
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  7. Article
  8. Review
  9. The Origin of Translation: Bridging the Nucleotides and Peptides.International journal of molecular sciences · 2022
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. tRNA Metabolism and Neurodevelopmental Disorders.Annual review of genomics and human genetics · 2019
    Review
  17. Review
  18. Ribosome Evolution and Structural Capacitance.Frontiers in molecular biosciences · 2019
    Article
  19. Article
  20. In the Beginning was a Mutualism - On the Origin of Translation.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2018
    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

2 authors at 1 institution in 1 country.

Charles W CarterDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260 carter@med.unc.edu water@med.unc.edu.
Richard WolfendenDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599-7260 carter@med.unc.edu water@med.unc.edu.
University of North Carolina at Chapel Hill · US

Funding

CHEMICAL MECHANISMS OF BIOSYNTHESISR01GM018325 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI WOLFENDEN, RICHARD VANCE · 1985 to 2011
$4.0M
Sense/Antisense Genetic Coding and the Origins of TranslationR01GM078227 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CARTER, CHARLES W. · 2006 to 2018
$3.9M
CHEMICAL MECHANISMS OF BIOSYNTHESISR37GM018325 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI WOLFENDEN, RICHARD VANCE · 1990 to 1999
–
NIGMS NIH HHS GM18325NIGMS NIH HHS GM78227NIGMS NIH HHS R01 GM018325NIGMS NIH HHS R01 GM078227NIGMS NIH HHS R37 GM018325
6 · The paper itself

Abstract

Aminoacyl-tRNA synthetases recognize tRNA anticodon and 3' acceptor stem bases. Synthetase Urzymes acylate cognate tRNAs even without anticodon-binding domains, in keeping with the possibility that acceptor stem recognition preceded anticodon recognition. Representing tRNA identity elements with two bits per base, we show that the anticodon encodes the hydrophobicity of each amino acid side-chain as represented by its water-to-cyclohexane distribution coefficient, and this relationship holds true over the entire temperature range of liquid water. The acceptor stem codes preferentially for the surface area or size of each side-chain, as represented by its vapor-to-cyclohexane distribution coefficient. These orthogonal experimental properties are both necessary to account satisfactorily for the exposed surface area of amino acids in folded proteins. Moreover, the acceptor stem codes correctly for β-branched and carboxylic acid side-chains, whereas the anticodon codes for a wider range of such properties, but not for size or β-branching. These and other results suggest that genetic coding of 3D protein structures evolved in distinct stages, based initially on the size of the amino acid and later on its compatibility with globular folding in water.

Indexed as

Protein FoldingAmino Acyl-tRNA SynthetasesAnticodonBinding SitesEvolution, MolecularGenetic CodeHydrophobic and Hydrophilic InteractionsModels, GeneticModels, MolecularNucleic Acid ConformationRegression AnalysisRNA, TransferThermodynamicsAmino Acyl-tRNA SynthetasesAnticodonRNA, Transferaminoacyl-tRNA synthetasesgenetic codemultivariate regressionprotein foldingurzymes

Identifiers

PMID26034281
PMCPMC4475997
OpenAlexW1584672266

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.