Evidence map›Paper›PMID 34094214›Full record

ArticleChemical science2020

Increasing protein stability by engineering the n → π* interaction at the β-turn.

Bhavesh Khatri, Puja Majumder, Jayashree Nagesh, Aravind Penmatsa, Jayanta Chatterjee

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
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  4. Aromatic-Carbonyl Interactions as an Emerging Type of Non-Covalent Interactions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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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 at 2 institutions in 2 countries.

Bhavesh KhatriMolecular Biophysics Unit, Indian Institute of Science Bangalore 560012 India penmatsa@iisc.ac.in jayanta@iisc.ac.in.ORCID https://orcid.org/0000-0002-3603-7839
Puja MajumderMolecular Biophysics Unit, Indian Institute of Science Bangalore 560012 India penmatsa@iisc.ac.in jayanta@iisc.ac.in.ORCID https://orcid.org/0000-0002-5421-6814
Jayashree NageshSolid State and Structural Chemistry Unit, Indian Institute of Science Bangalore India.ORCID https://orcid.org/0000-0002-0415-8329
Aravind PenmatsaMolecular Biophysics Unit, Indian Institute of Science Bangalore 560012 India penmatsa@iisc.ac.in jayanta@iisc.ac.in.ORCID https://orcid.org/0000-0001-9519-5055
Jayanta ChatterjeeMolecular Biophysics Unit, Indian Institute of Science Bangalore 560012 India penmatsa@iisc.ac.in jayanta@iisc.ac.in.ORCID https://orcid.org/0000-0002-4124-7339
Institute of Molecular Biology and Biophysics · RUIndian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Abundant n → π* interactions between adjacent backbone carbonyl groups, identified by statistical analysis of protein structures, are predicted to play an important role in dictating the structure of proteins. However, experimentally testing the prediction in proteins has been challenging due to the weak nature of this interaction. By amplifying the strength of the n → π* interaction

Identifiers

PMID34094214
PMCPMC8161691
OpenAlexW3046516409

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.