Leszek Konieczny
Overview
Explore the profile of Leszek Konieczny including associated specialties, affiliations and a list of published articles.
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86
Citations
498
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Recent Articles
1.
Roterman I, Slupina M, Konieczny L
Comput Struct Biotechnol J
. 2024 Nov;
23:3827-3838.
PMID: 39525086
The spatial structure of proteins, largely determined by their amino acid sequences, is also dependent on the environmental conditions under which the folding process takes place. In aqueous environments, exposure...
2.
Roterman I, Stapor K, Dulak D, Konieczny L
FEBS Open Bio
. 2024 Oct;
14(12):2006-2025.
PMID: 39370305
The domain-swapping mechanism involves the exchange of structural elements within a secondary or supersecondary structure between two (or more) proteins. The present paper proposes to interpret the domain-swapping mechanism using...
3.
Roterman I, Slupina M, Stapor K, Konieczny L, Gadek K, Nowakowski P
ACS Omega
. 2024 Sep;
9(37):38506-38522.
PMID: 39310170
Repeated protein folding processes both in vivo and in vitro leading to the same structure for a specific amino acid sequence prove that the amino acid sequence determines protein structuring....
4.
Roterman I, Stapor K, Dulak D, Konieczny L
ACS Omega
. 2024 Apr;
9(16):18412-18428.
PMID: 38680295
The present study discusses the influence of the TRiC chaperonin involved in the folding of the component of reovirus mu1/σ3. The TRiC chaperone is treated as a provider of a...
5.
Roterman I, Stapor K, Konieczny L
Front Chem
. 2024 Apr;
12:1342434.
PMID: 38595701
The protein folding process is very sensitive to environmental conditions. Many possibilities in the form of numerous pathways for this process can-if an incorrect one is chosen-lead to the creation...
6.
Roterman I, Konieczny L, Stapor K, Slupina M
ACS Omega
. 2024 Feb;
9(7):8188-8203.
PMID: 38405467
The biocatalysis process takes place with the participation of enzymes, which, depending on the reaction carried out, require, apart from the appropriate arrangement of catalytic residues, an appropriate external force...
7.
Lasota M, Zemanek G, Barczyk-Woznicka O, Misterka A, Wisniewska A, Stopa B, et al.
Nanomedicine (Lond)
. 2024 Jan;
19(4):281-292.
PMID: 38240228
FeT is a complex of Fe, ferricyanide and tartrate, similar in structure to Prussian Blue. Its synthesis was planned to produce a potential antiproliferative drug. Dynamic light scattering was applied...
8.
Roterman I, Stapor K, Konieczny L
Proteins
. 2023 Dec;
92(5):593-609.
PMID: 38062872
Transmembrane proteins are active in amphipathic environments. To stabilize the protein in such surrounding the exposure of hydrophobic residues on the protein surface is required. Transmembrane proteins are responsible for...
9.
Roterman I, Stapor K, Konieczny L
BMC Bioinformatics
. 2023 Nov;
24(1):425.
PMID: 37950210
Background: Recently, significant progress has been made in the field of protein structure prediction by the application of artificial intelligence techniques, as shown by the results of the CASP13 and...
10.
Roterman I, Stapor K, Konieczny L
BMC Bioinformatics
. 2023 Nov;
24(1):418.
PMID: 37932669
Background: The aqueous environment directs the protein folding process towards the generation of micelle-type structures, which results in the exposure of hydrophilic residues on the surface (polarity) and the concentration...