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摘要翻译：
热力学标度理论以前主要应用于小蛋白质，这里分析了标题为功能网络巨枢纽酶的定量进化。同源性鉴定的宽域结构仅用氨基酸序列进行水病理证实。最令人惊讶的结果是酪氨酸激酶球状表面粗糙度从鸟类到哺乳动物的进化是一级的，而哺乳动物从啮齿类到人类的进化是二级的。原癌基因酪氨酸蛋白激酶独特的酰胺末端区之谜通过在那里发现一个septad靶向簇而被解开，该簇与人类和其他一些物种的酪氨酸激酶中的八tad催化簇类似。这些结果很大程度上解释了为什么这些蛋白质是蛋白质相互作用网络中最大的巨型中枢之一，但没有使用可调节的参数。
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英文标题：
《Giant Hub Src and Syk Tyrosine Kinase Thermodynamic Profiles
Recapitulate Evolution》
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作者：
J. C. Phillips
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最新提交年份：
2016
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分类信息：
一级分类：Quantitative Biology 数量生物学
二级分类：Other Quantitative Biology 其他定量生物学
分类描述：Work in quantitative biology that does not fit into the other q-bio classifications
不适合其他q-bio分类的定量生物学工作
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英文摘要：
Thermodynamic scaling theory, previously applied mainly to small proteins, here analyzes quantitative evolution of the titled functional network giant hub enzymes. The broad domain structure identified homologically is confirmed hydropathically using amino acid sequences only. The most surprising results concern the evolution of the tyrosine kinase globular surface roughness from avian to mammals, which is first order, compared to the evolution within mammals from rodents to humans, which is second order. The mystery of the unique amide terminal region of proto oncogene tyrosine protein kinase is resolved by the discovery there of a septad targeting cluster, which is paralleled by an octad catalytic cluster in tyrosine kinase in humans and a few other species. These results, which go far towards explaining why these proteins are among the largest giant hubs in protein interaction networks, use no adjustable parameters.
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PDF链接：
https://arxiv.org/pdf/1610.04656
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