Evidence map›Paper›PMID 33175508›Full record

ArticleBiochemistry2020

Polyamines Mediate Folding of Primordial Hyperacidic Helical Proteins.

Dragana Despotović, Liam M Longo, Einav Aharon, Amit Kahana, Tali Scherf, Ita Gruic-Sovulj, Dan S Tawfik

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 18% 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, 30 citations in OpenAlex.

  1. Article
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  5. Review
  6. Article
  7. Article
  8. Origins of Life: The Protein Folding Problem all over again?Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Peptides En Route from Prebiotic to Biotic Catalysis.Accounts of chemical research · 2024
    Article
  10. Article
  11. Article
  12. Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains.Journal of the American Chemical Society · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. 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

7 authors at 3 institutions in 4 countries.

Dragana DespotovićDepartment of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Liam M LongoDepartment of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Einav AharonDepartment of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Amit KahanaDepartment of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Tali ScherfDepartment of Chemical Research Support, Weizmann Institute of Science, 7610001 Rehovot, Israel.
Ita Gruic-SovuljDepartment of Chemistry, Faculty of Science, University of Zagreb, 10000 Zagreb, Croatia.
Dan S TawfikDepartment of Biomolecular Sciences, Weizmann Institute of Science, 7610001 Rehovot, Israel.ORCID 0000-0002-5914-8240
Weizmann Institute of Science · ILTokyo Institute of Technology · JPUniversity of Zagreb · HR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyamines are known to mediate diverse biological processes, and specifically to bind and stabilize compact conformations of nucleic acids, acting as chemical chaperones that promote folding by offsetting the repulsive negative charges of the phosphodiester backbone. However, whether and how polyamines modulate the structure and function of proteins remain unclear. In particular, early proteins are thought to have been highly acidic, like nucleic acids, due to a scarcity of basic amino acids in the prebiotic context. Perhaps polyamines, the abiotic synthesis of which is simple, could have served as chemical chaperones for such primordial proteins? We replaced all lysines of an ancestral 60-residue helix-bundle protein with glutamate, resulting in a disordered protein with 21 glutamates in total. Polyamines efficiently induce folding of this hyperacidic protein at submillimolar concentrations, and their potency scaled with the number of amine groups. Compared to cations, polyamines were several orders of magnitude more potent than Na

Indexed as

Amino Acid SubstitutionCircular DichroismGlutamic AcidHydrogen-Ion ConcentrationLysineNuclear Magnetic Resonance, BiomolecularPolyaminesProtein FoldingProteinsGlutamic AcidLysinePolyaminesProteins

Identifiers

PMID33175508
PMCPMC7735664
OpenAlexW3098800017

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.