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
Descripción
Sumario: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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