Evidence map›Paper›PMID 42080292›Full record

ArticleProtein science : a publication of the Protein Society2026

The interplay between the pyramidalization of carbonyl carbons and the n → π* interactions in biomolecules.

Luigi Vitagliano, Luciana Esposito

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Luigi VitaglianoInstitute of Biostructures and Bioimaging, CNR, Naples, Italy.
Luciana EspositoInstitute of Biostructures and Bioimaging, CNR, Naples, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The structural preferences of biomolecules arise from a delicate balance of different forces whose identification and quantification are challenging. Studies conducted over the last two decades have shown that the n → π* interaction formed between consecutive carbonyl groups plays a crucial role in stabilizing biomolecules, which exhibit a wide range of chemical properties and structural complexities. These studies also demonstrate that the n → π* interaction relies heavily on the pyramidalization of the carbonyl group, which accepts electrons, to such an extent that pyramidalization has frequently been considered a signature of this interaction. Here, statistical surveys of different structural databases aimed at evaluating the precise relationship between the n → π* interaction and the carbonyl carbon pyramidalization (θ

Indexed as

CarbonProteinsModels, MolecularCarbonProteinscarbonyl carbon pyramidalizationconformational pre‐organizationconformation‐dependent geometrynon‐covalent interactions in biomolecules

Identifiers

PMID42080292
PMCPMC13137273

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.