Evidence map›Paper›PMID 40415290›Full record

ArticleProtein and peptide letters2025

Design, Expression, and Purification of a Fusion Enzyme Containing Terminal Deoxynucleotidyl Transferase from

Antos Sachanka, Veronika Shchur, Yaraslau Dzichenka, Aleksei Yantsevich

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Article in Protein and peptide letters, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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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

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No citing paper in PubMed yet.

4 · The record

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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

4 authors.

Antos SachankaInstitute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus.ORCID 0000-0001-8198-0909
Veronika ShchurInstitute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus.
Yaraslau DzichenkaInstitute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus.
Aleksei YantsevichInstitute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus.

Funding

Belorussian Fund for Fundamental Research X2021M-056National Academy of Science of Belarus 2023-27-021, 20210422
6 · The paper itself

Abstract

backgroundGene fusion techniques have yielded promising results in the fusion of thermostable polymerases (Taq and Pfu) with single-stranded and double-stranded DNA-binding proteins. Constructing a terminal deoxynucleotidyl transferase (TdT) fusion enzyme with DNAbinding protein domains can enhance thermostability and broaden the enzyme's application field. This makes it a promising candidate for cost-effective

methodsThe design of fusion proteins was based on molecular dynamics and homology modeling. Native and fusion proteins were isolated using affinity chromatography on HisTrap HP. Thermostability was assessed through differential scanning fluorimetry and dynamic light scattering. HPLC analysis was conducted to evaluate enzyme activity.

resultsAccording to the

conclusionThe fusion of TdT with EcSSB resulted in increased thermal stability and a reduced ability to add nucleotides to the substrate.

Indexed as

DNA-Binding ProteinsDNA NucleotidylexotransferaseEscherichia coliEscherichia coli ProteinsRecombinant Fusion ProteinsEnzyme StabilityMolecular Dynamics SimulationDNA-Binding ProteinsDNA NucleotidylexotransferaseEscherichia coli ProteinsRecombinant Fusion Proteinsdifferential scanning fluorimetrydynamic light scattering.EcSSBFusion proteinsingle-strand DNA-binding proteinsterminal deoxynucleotidyl transferase

Identifiers

PMID40415290

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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.