Evidence map›Paper›PMID 38100281›Full record

ArticleProtein science : a publication of the Protein Society2024

Emerging role of carbonyl-carbonyl interactions in the classification of beta turns.

Nancy D'Arminio, Valentina Ruggiero, Giovanni Pierri, Anna Marabotti, Consiglia Tedesco

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

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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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Geometric descriptors for beta turns.Protein science : a publication of the Protein Society · 2024
    Article
  4. Emerging role of carbonyl-carbonyl interactions in the classification of beta turns.Protein science : a publication of the Protein Society · 2024
    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

5 authors.

Nancy D'ArminioDepartment of Chemistry and Biology "A. Zambelli", University of Salerno, Fisciano, Italy.
Valentina RuggieroDepartment of Chemistry and Biology "A. Zambelli", University of Salerno, Fisciano, Italy.
Giovanni PierriDepartment of Chemistry and Biology "A. Zambelli", University of Salerno, Fisciano, Italy.
Anna MarabottiDepartment of Chemistry and Biology "A. Zambelli", University of Salerno, Fisciano, Italy.ORCID 0000-0002-9510-5205
Consiglia TedescoDepartment of Chemistry and Biology "A. Zambelli", University of Salerno, Fisciano, Italy.

Funding

Banca d'ItaliaMinistero dell'Istruzione, dell'Università e della Ricerca PRIN2017483NH8Ministero dell'Università e della Ricerca P2022ZBNC2Ministero dell'Università e della Ricerca PRIN2022-PNRRUniversità degli Studi di Salerno
6 · The paper itself

Abstract

Carbonyl-carbonyl interactions in peptides and proteins attracted considerable interest in recent years. Here, we report a survey of carbonyl-carbonyl interactions in cyclic peptides, depsipeptides, peptoids and discuss the relationship between backbone torsion angles and CO∙∙∙CO distances. In general, φ values in the range between -40° and -90° and between 40° and 90° correspond to CO∙∙∙CO distances below 3.22 Å. By extending the analysis of carbonyl-carbonyl interactions in different types of beta turns in proteins, we also highlight the role of direct or reciprocal carbonyl-carbonyl interactions in stabilizing the beta turn conformation for each specific type. We confirmed the new type II beta turn, detected by Dunbrack and coworkers, and named Pa, and detect the presence of a direct carbonyl-carbonyl interaction between the second and third residues of the turn. We also evidenced the existence of another new type II beta turn, named pA (following Dunbrack's notation), which represents the alternative conformation of Pa with opposite φ and ψ values and is characterized by a direct carbonyl-carbonyl interaction between the second and third residues of the turn. Finally, we show that the occurrence of CO∙∙∙CO interactions could be also advocated to explain from a chemical point of view the diversity of turn types.

Indexed as

PeptidesProteinsHydrogen BondingPeptides, CyclicProtein ConformationPeptidesPeptides, CyclicProteinsbackbone torsion anglesbeta turnscarbonyl-carbonyl interactionspeptoidsprotein structuresecondary structures

Identifiers

PMID38100281
PMCPMC10806932

What OpenQuestion holds

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Read underepoch 390

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.