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Ligation site in proteins recognized in silico.

ABSTRACT: UNLABELLED: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.

SUBMITTER: Brylinski M

PROVIDER: S-EPMC1891674 | biostudies-literature | 2006 Apr

REPOSITORIES: biostudies-literature

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Ligation site in proteins recognized in silico.

Brylinski Michal M Konieczny Leszek L Roterman Irena I

Bioinformation 20060411 4

<h4>Unlabelled</h4>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 s ...[more]

PMID: 17597871

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