Evidence map›Paper›PMID 31908743›Full record

ArticleAvicenna journal of medical biotechnology

Importance of Fluctuating Amino Acid Residues in Folding and Binding of Proteins.

Renganathan Senthil, Singaravelu Usha, Konda Mani Saravanan

Open access · greenAbstract read
In one paragraph

Article in Avicenna journal of medical biotechnology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.1field-weighted citation impact, top 52% 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

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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

5 citing papers in PubMed, 12 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Renganathan SenthilDepartment of Bioinformatics, Faculty of Biosciences, The Marudupandiyar Institutions, Thanjavur-613403, Tamil Nadu, India.
Singaravelu UshaDepartment of Bioinformatics, Bharathiar University, Coimbatore-641046, Tamil Nadu, India.
Konda Mani SaravananDepartment of Bioinformatics, Faculty of Biosciences, The Marudupandiyar Institutions, Thanjavur-613403, Tamil Nadu, India.
Bharathiar University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundConformational flexibility of proteins remains as one of the major events in protein-protein/DNA/ligand/small molecule binding to achieve its biological function in the cell. The availability of high-resolution structures of protein complexes is a valuable resource for researchers to understand the mechanisms behind such interactions and it is found that the flexibility of amino acid residues at binding sites is crucial for many important functions in the cell.

methodsIn this article, our statistical method (PreFRP) developed based on fluctuating amino acid residues and various amino acid indices related to flexibility/rigidity were used to study the importance of fluctuating amino acid residues in thermonucleases from pathogenic bacteria, cell penetrating peptides and intrinsically disordered proteins responsible for many neural disorders.

resultsThe results from our analysis reveal the importance of fluctuating amino acid residues in folding and binding of proteins. The role of moderate and high fluctuating residues in themonucleases, cell penetrating peptide and disordered regions are discussed in detail.

conclusionTherefore, our analysis will help in understanding the importance of fluctuating amino acid residues in proteins which undergo a conformation change phenomenon.

Indexed as

Amino acidBinding sitesCell-penetrating peptidesDNA-binding proteins

Identifiers

PMID31908743
PMCPMC6925403
OpenAlexW2979892338

What OpenQuestion holds

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LicenceCC BY
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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.