Bioinformatics Advance Access originally published online on January 19, 2005
Bioinformatics 2005 21(8):1311-1315; doi:10.1093/bioinformatics/bti167
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Topology of small-world networks of proteinprotein complex structures
Bioinformatics Research Project, Research and Development Division, Fujirebio Inc. 51 Komiya-cho, Hachioji-shi, Tokyo 192-0031, Japan
*To whom correspondence should be addressed.
The majority of real examples of small-world networks exhibit a power law distribution of edges among the nodes, therefore not fitting into the wiring model proposed by Watts and Strogatz. However, protein structures can be modeled as small-world networks, with a distribution of the number of links decaying exponentially as in the case of this wiring model. We approach the proteinprotein interaction mechanism by viewing it as a particular rewiring occurring in the system of two small-world networks represented by the monomers, where a re-arrangement of links takes place upon dimerization leaving the small-world character in the dimer network. Due to this rewiring, the most central residues at the complex interfaces tend to form clusters, which are not homogenously distributed. We show that these highly central residues are strongly correlated with the presence of hot spots of binding free energy.
Contact: ao-mesa{at}fujirebio.co.jp
Supplementary information: http://www.fujirebio.co.jp/support/index.php (under construction).
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