Title

Ligation site in proteins recognized in silico

Authors

Michal Brylinski^1,2, Leszek Konieczny³, Irena Roterman^1,4,*

Affiliation

¹Department of Bioinformatics and Telemedicine, Collegium Medicum – Jagiellonian University, Kopernika 17, 31-501 Krakow, Poland; ²Faculty of Chemistry, Jagiellonian University, Ingardena 3, 30-060 Krakow, Poland; ³Institute of Medical Biochemistry, Collegium Medicum – Jagiellonian University, Kopernika 7, 31 034 Krakow, Poland; ⁴Faculty of Physics, Jagiellonian University, Reymonta 4, 30-060 Krakow, Poland

E-mail*

myroterm@cyf-kr.edu.pl; * Corresponding author

Article Type

Current Trends

Date

received March 27, 2006; accepted April 5, 2006; published online April 11, 2006

Abstract

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

Keywords

hydrophobicity; active site; function recognition; protein structure

Citation

Brylinski et al., Bioinformation 1(4): 127-129 (2006)

Edited by

P. Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.