Evidence map›Paper›PMID 41665198›Full record

ArticleThe FEBS journal2026

Comparative evaluation of noncanonical amino acids as site-specific NMR probes for the complex of E. coli SSB with single-stranded DNA without isotope labelling.

Sreelakshmi Mekkattu Tharayil, Haocheng Qianzhu, Elwy H Abdelkader, Adarshi P Welegedara, Josemon George, Christoph Nitsche, Thomas Huber, Gottfried Otting

Abstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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.

Sreelakshmi Mekkattu TharayilResearch School of Chemistry, The Australian National University, Canberra, Australia.
Haocheng QianzhuResearch School of Chemistry, The Australian National University, Canberra, Australia.
Elwy H AbdelkaderCentre of Excellence for Innovations in Peptide and Protein Science, Research School of Chemistry, The Australian National University, Canberra, Australia.
Adarshi P WelegedaraCentre of Excellence for Innovations in Peptide and Protein Science, Research School of Chemistry, The Australian National University, Canberra, Australia.
Josemon GeorgeResearch School of Chemistry, The Australian National University, Canberra, Australia.
Christoph NitscheResearch School of Chemistry, The Australian National University, Canberra, Australia.
Thomas HuberResearch School of Chemistry, The Australian National University, Canberra, Australia.
Gottfried OttingCentre of Excellence for Innovations in Peptide and Protein Science, Research School of Chemistry, The Australian National University, Canberra, Australia.ORCID https://orcid.org/0000-0002-0563-0146

Funding

Australian Research Council CE200100012Australian Research Council DP230100079
6 · The paper itself

Abstract

The binding of tetrameric E. coli single-stranded DNA-binding protein (SSB) to single-stranded DNA (ssDNA) was investigated using genetically encoded noncanonical amino acids (ncAA) as site-specific probes for detection by nuclear magnetic resonance (NMR) spectroscopy. Under the conditions used (300 mm NaCl, pH 7.2), the NMR spectra confirmed the equivalence of the monomeric subunits in the absence of ssDNA. Most of the probes responded to the binding of ssDNA by changes in chemical shifts and line width and distinguished between the presence of segments of cytidine versus thymidine. Although ssDNA-binding breaks the fourfold symmetry of the SSB tetramer, the probes sensed closely similar chemical environments in all four monomeric subunits. By comparing the performance of twelve different NMR-active ncAAs, this work identified N

Indexed as

Amino AcidsDNA-Binding ProteinsDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsAmino Acyl-tRNA SynthetasesIsotope LabelingLysineMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein BindingTyrosineAmino AcidsAmino Acyl-tRNA SynthetasesDNA-Binding ProteinsDNA, Single-StrandedEscherichia coli ProteinsLysineSSB protein, E coliTyrosine19F‐NMR spectroscopyE. coli single‐stranded DNA‐binding protein (SSB)genetic encodingnoncanonical amino acidsnuclear magnetic resonance (NMR)

Identifiers

PMID41665198
PMCPMC13278363

What OpenQuestion holds

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Registered trials

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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.