Partner: Irena Roterman-Konieczna

Jagiellonian University (PL)

Promotor prac doktorskich
1.2018-05-24Banach Mateusz  
(UJ)
Metody obliczeniowe jedno- i wielokryterialnej optymalizacji rojem cząstek. Zastosowanie w bioinformatyce 

Ostatnie publikacje
1.Prymula K., Piwowar M., Kochańczyk M., Flis Ł., Malawski M., Szepieniec T., Evangelista G., Minervini G., Polticelli F., Wiśniowski Z., Sałapa K., Matczyńska E., Roterman I., In silico Structural Study of Random Amino Acid Sequence Proteins Not Present in Nature, CHEMISTRY AND BIODIVERSITY, ISSN: 1612-1872, DOI: 10.1002/cbdv.200800338, Vol.6, No.12, pp.2311-2336, 2009

Streszczenie:

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.

Afiliacje autorów:

Prymula K.-other affiliation
Piwowar M.-other affiliation
Kochańczyk M.-IPPT PAN
Flis Ł.-Jagiellonian University (PL)
Malawski M.-AGH University of Science and Technology (PL)
Szepieniec T.-Academic Computer Center CYFRONET (PL)
Evangelista G.-Universita degli Studi Roma Tre (IT)
Minervini G.-Universita degli Studi Roma Tre (IT)
Polticelli F.-Universita degli Studi Roma Tre (IT)
Wiśniowski Z.-Jagiellonian University (PL)
Sałapa K.-Jagiellonian University (PL)
Matczyńska E.-Jagiellonian University (PL)
Roterman I.-Jagiellonian University (PL)
20p.
2.Bryliński M., Kochańczyk M., Broniatowska E., Roterman I., Localization of ligand binding site in proteins identified in silico, Journal of Molecular Modeling, ISSN: 1610-2940, DOI: 10.1007/s00894-007-0191-x, Vol.13, No.6, pp.665-675, 2007

Streszczenie:

Knowledge-based models for protein folding assume that the early-stage structural form of a polypeptide is determined by the backbone conformation, followed by hydrophobic collapse. Side chain–side chain interactions, mostly of hydrophobic character, lead to the formation of the hydrophobic core, which seems to stabilize the structure of the protein in its natural environment. The fuzzy-oil-drop model is employed to represent the idealized hydrophobicity distribution in the protein molecule. Comparing it with the one empirically observed in the protein molecule reveals that they are not in agreement. It is shown in this study that the irregularity of hydrophobic distributions is aim-oriented. The character and strength of these irregularities in the organization of the hydrophobic core point to the specificity of a particular protein’s structure/function. When the location of these irregularities is determined versus the idealized fuzzy-oil-drop, function-related areas in the protein molecule can be identified. The presented model can also be used to identify ways in which protein–protein complexes can possibly be created. Active sites can be predicted for any protein structure according to the presented model with the free prediction server at http://www.bioinformatics.cm-uj.krakow.pl/activesite. The implication based on the model presented in this work suggests the necessity of active presence of ligand during the protein folding process simulation.

Słowa kluczowe:

Hydrophobic collapse, Protein folding, Active site, Ligand binding

Afiliacje autorów:

Bryliński M.-other affiliation
Kochańczyk M.-IPPT PAN
Broniatowska E.-other affiliation
Roterman I.-Jagiellonian University (PL)
3.Bryliński M., Prymula K., Jurkowski W., Kochańczyk M., Stawowczyk E., Konieczny L., Roterman I., Prediction of Functional Sites Based on the Fuzzy Oil Drop Model, PLOS COMPUTATIONAL BIOLOGY, ISSN: 1553-7358, DOI: 10.1371/journal.pcbi.0030094, Vol.3, No.5, pp.e94-0909-0923, 2007

Streszczenie:

A description of many biological processes requires knowledge of the 3-D structure of proteins and, in particular, the defined active site responsible for biological function. Many proteins, the genes of which have been identified as the result of human genome sequencing, and which were synthesized experimentally, await identification of their biological activity. Currently used methods do not always yield satisfactory results, and new algorithms need to be developed to recognize the localization of active sites in proteins. This paper describes a computational model that can be used to identify potential areas that are able to interact with other molecules (ligands, substrates, inhibitors, etc.). The model for active site recognition is based on the analysis of hydrophobicity distribution in protein molecules. It is shown, based on the analyses of proteins with known biological activity and of proteins of unknown function, that the region of significantly irregular hydrophobicity distribution in proteins appears to be function related.

Słowa kluczowe:

Protein structure, Amino acid analysis, Isomerases, Protein structure prediction, Genomic databases, Structural genomics, Protein structure comparison, Oils

Afiliacje autorów:

Bryliński M.-other affiliation
Prymula K.-other affiliation
Jurkowski W.-other affiliation
Kochańczyk M.-IPPT PAN
Stawowczyk E.-other affiliation
Konieczny L.-other affiliation
Roterman I.-Jagiellonian University (PL)
4.Bryliński M., Kochańczyk M., Konieczny L., Roterman I., Sequence-structure-function relation characterized in silico, In Silico Biology, ISSN: 1386-6338, Vol.6, No.6, pp.589-600, 2006

Słowa kluczowe:

Hydrophobicity, biological function, active site, proteins of unknown biological function

Afiliacje autorów:

Bryliński M.-other affiliation
Kochańczyk M.-IPPT PAN
Konieczny L.-other affiliation
Roterman I.-Jagiellonian University (PL)