Evidence map›Paper›PMID 40261918›Full record

ArticlePloS one2025

Chameleon sequences-Structural effects.

Mateusz Slupina, Katarzyna Stapor, Leszek Konieczny, Krzysztof Gądek, Piotr Nowakowski, Irena Roterman

Abstract read
In one paragraph

Article in PloS one, 2025. 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

6 authors.

Mateusz SlupinaALSTOM ZWUS Sp. z o.o. Modelarska, Katowice, Poland.
Katarzyna StaporFaculty of Automatic, Electronics and Computer Science, Department of Applied Informatics, Silesian University of Technology, Gliwice, Poland.ORCID 0000-0003-3003-6592
Leszek KoniecznyChair of Medical Biochemistry, Jagiellonian University - Medical College, Krakow, Poland.
Krzysztof GądekSano Centre for Computational Medicine, Kraków, Poland.
Piotr NowakowskiSano Centre for Computational Medicine, Kraków, Poland.
Irena RotermanDepartment of Bioinformatics and Telemedicine, Jagiellonian University -Medical College, Krakow, Poland.ORCID 0000-0003-3652-9099

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The predisposition of amino acids towards accepting the appropriate secondary structure form is ambiguous. The identified sequences (6-12 aa in length - ChSeq data base) of the chameleon type (the same sequence accepting different secondary structures) constitute a puzzle that makes it difficult to indicate the initial conformation in a chain with a given amino acid sequence. The analysis of proteins presented in this paper uses the hydrophobicity distribution in protein body as the criterion for comaparable analysis of the status of helica/Beta-structural chameleon fragments in pairs of proteins. The sub-base is the object of analysis containg the proteins representing the organisation of hydrophobicity in one protein of the pair as ordered according to micelle-like organisation (hydrophobic core with polar surface) and the second one in pair with disordered hydrophobicity organisation. The status of chameleon sections appears to represent local organisation of hydrophobicity highly accordant in both proteins in chameleon pair independently on the status of the structural unit they belong to. The fuzzy oil drop model (FOD) in its modified form (FOD-M) is applied for analysis. This work aims to verify the hypothesis assuming the subordination of the form of secondary structure to the superior goal of obtaining a hydrophobicity distribution suitable for the given biological activity of the protein, ensuring biological functionality. Secondary structure is not an aim by itself. It is shown, that the main goal is to reach the structure representing specific activity. Secondary structure is a means to achieve this goal.

Indexed as

ProteinsAmino Acid SequenceHydrophobic and Hydrophilic InteractionsModels, MolecularProtein Structure, SecondaryProteins

Identifiers

PMID40261918
PMCPMC12013887

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.