Abstract | ||
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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. |
Year | DOI | Venue |
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2007 | 10.1371/journal.pcbi.0030094 | PLOS COMPUTATIONAL BIOLOGY |
Keywords | Field | DocType |
biological activity,active site,amino acid sequence,protein binding,binding sites,algorithms,human genome,biological process,sequence alignment,fuzzy logic,protein structure,structural genomics,computer model,protein structure prediction,computer simulation | Sequence alignment,Protein structure prediction,Plasma protein binding,Structural genomics,Binding site,Biology,Function (biology),Active site,Bioinformatics,Protein structure | Journal |
Volume | Issue | ISSN |
3 | 5 | 1553-734X |
Citations | PageRank | References |
9 | 0.51 | 11 |
Authors | ||
7 |
Name | Order | Citations | PageRank |
---|---|---|---|
Michal Brylinski | 1 | 124 | 12.16 |
Katarzyna Prymula | 2 | 17 | 2.68 |
Wiktor Jurkowski | 3 | 18 | 3.14 |
Marek Kochanczyk | 4 | 17 | 2.89 |
Ewa Stawowczyk | 5 | 9 | 0.51 |
Leszek Konieczny | 6 | 67 | 22.55 |
Irena Roterman | 7 | 78 | 30.08 |