Ligation site in proteins recognized in silico

Recognition of a ligation site in a protein molecule is important for identifying its biological activity. The model for in silico recognition of ligation sites in proteins is presented. The idealized hydrophobic core stabilizing protein structure is represented by a three-dimensional Gaussian funct...

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Detalles Bibliográficos
Autores principales: Brylinski, Michal, Konieczny, Leszek, Roterman, Irena
Formato: Texto
Lenguaje:English
Publicado: Biomedical Informatics Publishing Group 2006
Materias:
Current Trends
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891674/
https://www.ncbi.nlm.nih.gov/pubmed/17597871
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author Brylinski, Michal
Konieczny, Leszek
Roterman, Irena
author_facet Brylinski, Michal
Konieczny, Leszek
Roterman, Irena
author_sort Brylinski, Michal
collection PubMed
description Recognition of a ligation site in a protein molecule is important for identifying its biological activity. The model for in silico recognition of ligation sites in proteins is presented. The idealized hydrophobic core stabilizing protein structure is represented by a three-dimensional Gaussian function. The experimentally observed distribution of hydrophobicity compared with the theoretical distribution reveals differences. The area of high differences indicates the ligation site. AVAILABILITY: http://bioinformatics.cm-uj.krakow.pl/activesite
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spelling pubmed-18916742007-06-27 Ligation site in proteins recognized in silico Brylinski, Michal Konieczny, Leszek Roterman, Irena Bioinformation Current Trends Recognition of a ligation site in a protein molecule is important for identifying its biological activity. The model for in silico recognition of ligation sites in proteins is presented. The idealized hydrophobic core stabilizing protein structure is represented by a three-dimensional Gaussian function. The experimentally observed distribution of hydrophobicity compared with the theoretical distribution reveals differences. The area of high differences indicates the ligation site. AVAILABILITY: http://bioinformatics.cm-uj.krakow.pl/activesite Biomedical Informatics Publishing Group 2006-04-11 /pmc/articles/PMC1891674/ /pubmed/17597871 Text en © 2006 Biomedical Informatics Publishing Group This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Current Trends
Brylinski, Michal
Konieczny, Leszek
Roterman, Irena
Ligation site in proteins recognized in silico
title Ligation site in proteins recognized in silico
title_full Ligation site in proteins recognized in silico
title_fullStr Ligation site in proteins recognized in silico
title_full_unstemmed Ligation site in proteins recognized in silico
title_short Ligation site in proteins recognized in silico
title_sort ligation site in proteins recognized in silico
topic Current Trends
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891674/
https://www.ncbi.nlm.nih.gov/pubmed/17597871
work_keys_str_mv AT brylinskimichal ligationsiteinproteinsrecognizedinsilico
AT koniecznyleszek ligationsiteinproteinsrecognizedinsilico
AT rotermanirena ligationsiteinproteinsrecognizedinsilico

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