Evidence map›Paper›PMID 28847940›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Surveying the sequence diversity of model prebiotic peptides by mass spectrometry.

Jay G Forsythe, Anton S Petrov, W Calvin Millar, Sheng-Sheng Yu, Ramanarayanan Krishnamurthy, Martha A Grover, Nicholas V Hud, Facundo M Fernández

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Protopeptide backbone affects assembly in aqueous solutions.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. From Catalysis of Evolution to Evolution of Catalysis.Accounts of chemical research · 2024
    Article
  12. Article
  13. Review
  14. Electron transport chains as a window into the earliest stages of evolution.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Toward Molecular Cooperation by De Novo Peptides.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2021
    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

8 authors.

Jay G ForsytheSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400.
Anton S PetrovSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400.
W Calvin MillarSchool of Physics, Georgia Institute of Technology, Atlanta, GA 30332-0430.
Sheng-Sheng YuSchool of Chemical & Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA 30332-0100.
Ramanarayanan KrishnamurthyDepartment of Chemistry, The Scripps Research Institute, La Jolla, CA 92037.
Martha A GroverSchool of Chemical & Biomolecular Engineering, Georgia Institute of Technology, Atlanta, GA 30332-0100.
Nicholas V HudSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400.
Facundo M FernándezSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332-0400; facundo.fernandez@chemistry.gatech.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The rise of peptides with secondary structures and functions would have been a key step in the chemical evolution which led to life. As with modern biology, amino acid sequence would have been a primary determinant of peptide structure and activity in an origins-of-life scenario. It is a commonly held hypothesis that unique functional sequences would have emerged from a diverse soup of proto-peptides, yet there is a lack of experimental data in support of this. Whereas the majority of studies in the field focus on peptides containing only one or two types of amino acids, here we used modern mass spectrometry (MS)-based techniques to separate and sequence de novo proto-peptides containing broader combinations of prebiotically plausible monomers. Using a dry-wet environmental cycling protocol, hundreds of proto-peptide sequences were formed over a mere 4 d of reaction. Sequence homology diagrams were constructed to compare experimental and theoretical sequence spaces of tetrameric proto-peptides. MS-based analyses such as this will be increasingly necessary as origins-of-life researchers move toward systems-level investigations of prebiotic chemistry.

Indexed as

Evolution, ChemicalOrigin of LifeAmino AcidsAmino Acid SequenceDepsipeptidesGenetic VariationMacromolecular SubstancesMass SpectrometryPeptidesProtein Structure, SecondarySequence Analysis, ProteinAmino AcidsDepsipeptidesMacromolecular SubstancesPeptideschemical evolutiondepsipeptidesmass spectrometrypeptidesprebiotic chemistry

Identifiers

PMID28847940
PMCPMC5604043

What OpenQuestion holds

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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.