We present a simple model for the underlying structure of protein–protein pairwise interaction graphs that is based on the way in which proteins attach to each other in experiments such as yeast two-hybrid assays. We show that data on the interactions of human proteins lend support to this model. The frequency of the number of connections per protein under this model does not follow a power law, in contrast to the reported behaviour of data from large-scale yeast two-hybrid screens of yeast protein–protein interactions. Sampling sub-graphs from the underlying graphs generated with our model, in a way analogous to the sampling performed in large-scale yeast two-hybrid searches, gives degree distributions that differ subtly from the power law and that fit the observed data better than the power law itself. Our results show that the observation of approximate power law behaviour in a sampled sub-graph does not imply that the underlying graph follows a power law.
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Conference Article| December 01 2003
On the structure of protein–protein interaction networks
A. Thomas ;
R. Cannings ;
N.A.M. Monk ;
N.A.M. Monk 1
‡Centre for Bioinformatics and Computational Biology, and Division of Genomic Medicine, University of Sheffield, Royal Hallamshire Hospital, Sheffield S10 2JF, U.K.
1To whom correspondence should be addressed (e-mail firstname.lastname@example.org).
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Biochem Soc Trans (2003) 31 (6): 1491–1496.
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A. Thomas, R. Cannings, N.A.M. Monk, C. Cannings; On the structure of protein–protein interaction networks. Biochem Soc Trans 1 December 2003; 31 (6): 1491–1496. doi: https://doi.org/10.1042/bst0311491
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