Infinite-order percolation and giant fluctuations in a protein interaction network
Infinite-order percolation and giant fluctuations in a protein interaction network
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DOI：
10.1103/physreve.66.055101
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发表时间：
2002-11-01
影响因子：
2.4
通讯作者：
Redner, S
中科院分区：
文献类型：
--
作者：
Kim, J;Krapivsky, PL;Redner, S
我们研究了一个模型蛋白质相互作用网络，其链接代表各个蛋白质之间的相互作用。该网络通过蛋白质的功能复制而进化，并通过随机链接添加来补充以解释突变。当链接加法占主导地位时，作为加法速率的函数，会出现无限阶渗流转变。在高重复率的相反限制下，网络在不同的实现中表现出巨大的结构波动。对于生物学相关的增长率，节点度分布具有代数尾部，且相关指数具有特殊的速率依赖性。
We investigate a model protein interaction network whose links represent interactions between individual proteins. This network evolves by the functional duplication of proteins, supplemented by random link addition to account for mutations. When link addition is dominant, an infinite-order percolation transition arises as a function of the addition rate. In the opposite limit of high duplication rate, the network exhibits giant structural fluctuations in different realizations. For biologically relevant growth rates, the node degree distribution has an algebraic tail with a peculiar rate dependence for the associated exponent.