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Dive into the research topics where Zdzisław Wiśniowski is active.

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Featured researches published by Zdzisław Wiśniowski.


Chemistry & Biodiversity | 2009

In silico Structural Study of Random Amino Acid Sequence Proteins Not Present in Nature

Katarzyna Prymula; Monika Piwowar; Marek Kochańczyk; Lukasz Flis; Maciej Malawski; Tomasz Szepieniec; Giovanni Evangelista; Giuseppe Minervini; Fabio Polticelli; Zdzisław Wiśniowski; Kinga Sałapa; Ewa Matczyńska; Irena Roterman

The three‐dimensional structures of a set of ‘never born proteins’ (NBP, random amino acid sequence proteins with no significant homology with known proteins) were predicted using two methods: Rosetta and the one based on the ‘fuzzy‐oil‐drop’ (FOD) model. More than 3000 different random amino acid sequences have been generated, filtered against the non redundant protein sequence data base, to remove sequences with significant homology with known proteins, and subjected to three‐dimensional structure prediction. Comparison between Rosetta and FOD predictions allowed to select the ten top (highest structural similarity) and the ten bottom (the lowest structural similarity) structures from the ranking list organized according to the RMS‐D value. The selected structures were taken for detailed analysis to define the scale of structural accordance and discrepancy between the two methods. The structural similarity measurements revealed discrepancies between structures generated on the basis of the two methods. Their potential biological function appeared to be quite different as well. The ten bottom structures appeared to be ‘unfoldable’ for the FOD model. Some aspects of the general characteristics of the NBPs are also discussed. The calculations were performed on the EUChinaGRID grid platform to test the performance of this infrastructure for massive protein structure predictions.


international conference on computational science | 2008

MPEG-7 as a Metadata Standard for Indexing of Surgery Videos in Medical E-Learning

Andrzej A. Kononowicz; Zdzisław Wiśniowski

The analysis of video recorded surgical procedures is considered to be a useful extension of the medical curriculum. We can foster the development of video-based e-learning courses by working out a unified description method which would facilitate the exchange of these materials between different platforms. Sophisticated metadata enables a broader integration of artificial intelligence techniques into e-learning. The aim of this paper is to present the possibility of combining the MPEG-7 metadata standard with the MeSH classification for indexing of video recordings in medical e-learning. A tool for metadata descriptions of surgical videos in accordance with the MPEG-7 standard is also presented. This tool is part of a larger architecture for the exchange of medical multimedia objects.


Bioinformation | 2008

Never born proteins as a test case for ab initio protein structures prediction

Giovanni Minervini; Giuseppe Evangelista; Fabricio Polticelli; Monika Piwowar; Marek Kochańczyk; Lukasz Flis; Maciej Malawski; Tomasz Szepieniec; Zdzisław Wiśniowski; Ewa Matczyńska; Katarzyna Prymula; Irena Roterman

The number of natural proteins although large is significantly smaller than the theoretical number of proteins that can be obtained combining the 20 natural amino acids, the so-called “never born proteins” (NBPs). The study of the structure and properties of these proteins allows to investigate the sources of the natural proteins being of unique characteristics or special properties. However the structural study of NPBs can also been intended as an ideal test for evaluating the efficiency of software packages for the ab initio protein structure prediction. In this research, 10.000 three-dimensional structures of proteins of completely random sequence generated according to ROSETTA and FOD model were compared. The results show the limits of these software packages, but at the same time indicate that in many cases there is a significant agreement between the prediction obtained.


Journal of Molecular Modeling | 2017

Is the hydrophobic core a universal structural element in proteins

Barbara Kalinowska; Mateusz Banach; Zdzisław Wiśniowski; Leszek Konieczny; Irena Roterman

The hydrophobic core, when subjected to analysis based on the fuzzy oil drop model, appears to be a universal structural component of proteins irrespective of their secondary, supersecondary, and tertiary conformations. A study has been performed on a set of nonhomologous proteins representing a variety of CATH categories. The presence of a well-ordered hydrophobic core has been confirmed in each case, regardless of the protein’s biological function, chain length or source organism. In light of fuzzy oil drop (FOD) analysis, various supersecondary forms seem to share a common structural factor in the form of a hydrophobic core, emerging either as part of the whole protein or a specific domain. The variable status of individual folds with respect to the FOD model reflects their propensity for conformational changes, frequently associated with biological function. Such flexibility is expressed as variable stability of the hydrophobic core, along with specific encoding of potential conformational changes which depend on the properties of helices and β-folds.


International Journal of Molecular Sciences | 2018

Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model

Dawid Dułak; Małgorzata Gadzała; Mateusz Banach; Magdalena Ptak; Zdzisław Wiśniowski; Leszek Konieczny; Irena Roterman

Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloid fibrils, meeting all the criteria defined under the fuzzy oil drop model in the context of amyloid characterization. The model recognizes amyloids as linear structures where local hydrophobicity minima and maxima propagate in an alternating manner along the fibril’s long axis. This distribution of hydrophobicity differs greatly from the classic monocentric hydrophobic core observed in globular proteins. Rather than becoming a globule, the amyloid instead forms a ribbonlike (or cylindrical) structure.


Bio-Algorithms and Med-Systems | 2018

Fragment Aβ(18-41) presented within the CDR3 loop region of a shark immunoglobulin new antigen receptor single-variable domain antibody analyzed based on the fuzzy oil drop model

Mateusz Banach; Leszek Konieczny; Zdzisław Wiśniowski; Irena Roterman

Abstract The structure of amyloid Aβ(1-41) is the object of many papers due to the neurodegenerative processes induced by this amyloid. One of the ways to investigate the possible structural forms other than the amyloid is to incorporate the fragment of this peptide into the chain of immunoglobulin. Fragment Aβ(18-41) presented within the CDR3 loop region of a shark immunoglobulin new antigen receptor single-variable domain antibody is the object of this analysis. The structure of this hybrid is available in the PDB and analyzed based on the fuzzy oil drop model. The aim is to define the status of this fragment, revealing the possible fitting to the ordered form of the hydrophobic core. Simultaneously, the verification of the predisposition to complexation is possible.


Bio-Algorithms and Med-Systems | 2018

Chromatin 3D – will it make understanding of cancer transformation finally possible?

Grażyna Drabik; Jolanta Kaszuba-Zwoińska; Zdzisław Wiśniowski; Leszek Konieczny; Irena Roterman

Abstract Despite enormous progress in molecular analysis of cancer cell genomes, the mechanism of tumorigenesis remains unclear. The information present in the genome is not limited to the DNA sequence itself. Indeed, a significant portion of this information is concealed in the spatial structure of chromatin. Ongoing scientific studies that focus on the three-dimensional structure of chromatin raise hopes of arriving at a general explanation of the cancer transformation phenomenon.


Geriatrics & Gerontology International | 2017

Effects of different rehabilitation models on erythrocyte deformability and nitrite plus nitrate as end-products of nitric oxide levels in elderly women

Katarzyna Filar-Mierzwa; Barbara Wójcik; Anna Marchewka; Zbigniew Dąbrowski; Jerzy Superata; Zdzisław Wiśniowski

The aim of the present study was to analyze the effects of two rehabilitation protocols, dance movement therapy exercises (DMT) and general rehabilitation exercises (GRE), on erythrocyte deformability and plasma levels of nitrite plus nitrate as end products of nitric oxide (NOx) in elderly women.


Bio-Algorithms and Med-Systems | 2017

Mechanism of ligand binding – PDZ domain taken as example

Dawid Dułak; Mateusz Banach; Zdzisław Wiśniowski; Leszek Konieczny; Irena Roterman

Abstract The mechanism of specific ligand binding by proteins is discussed using the PDZ domain complexing the pentapeptide. This process is critical for clustering the membrane ion channel. The traditional model based on the Beta-sheet extension by complexed pentapeptide is interpreted as a hydrophobic core extension supported by additional Beta-strand generated by complexed pentapeptide. The explanation is based on the fuzzy oil drop model applied to the crystal structure of PDZ-pentapeptide.


Bio-Algorithms and Med-Systems | 2017

The variability of protein structure with respect to the hydrophobic core

Mateusz Banach; Zdzisław Wiśniowski; Barbara Kalinowska; Leszek Konieczny; Irena Roterman

Abstract The application of the fuzzy oil drop model to the analysis of protein structure is shown using two proteins. The selection of these two examples is due to their opposite character. Two proteins were selected representing very high order and very high disorder with respect to the organized uni-central hydrophobic core in proteins (one centrally localized concentration of high hydrophobicity). These two cases are to show examples of the large spectrum of variability of local organization of the hydrophobic core in proteins. The importance of the observation presented in this paper is significant with respect to large sets of proteins discussed in separate publications.

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Irena Roterman

Jagiellonian University Medical College

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Ana Alekseenko

Jagiellonian University Medical College

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Jan Meus

Jagiellonian University

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