蛋白质的内在结构紊乱参与了相互作用组的进化。

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS ACS Applied Bio Materials Pub Date : 2024-10-20 DOI:10.1016/j.biosystems.2024.105351
Diego M. Bustos
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引用次数: 0

摘要

新的数学工具有助于了解细胞的功能、适应性和进化性,从而发现隐藏的变量,预测未来可在湿实验室进行测试的表型。不同的模型已被成功用于发现蛋白质-蛋白质相互作用网络或相互作用组的特性。我发现,在双曲线流行度-相似度模型中,结构内在无序度最高的细胞蛋白质在许多不同的真核生物相互作用组中聚集在一起,而原核生物大肠杆菌的情况并非如此,在大肠杆菌中,内在无序度高的蛋白质很少。我还发现,同源物蛋白质流行度-相似度模型的归一化θ变量与分析生物的复杂性相关。
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Intrinsic structural disorder on proteins is involved in the interactome evolution
New mathematical tools help understand cell functions, adaptability, and evolvability to discover hidden variables to predict phenotypes that could be tested in the future in wet labs. Different models have been successfully used to discover the properties of the protein-protein interaction networks or interactomes. I found that in the hyperbolic Popularity-Similarity model, cellular proteins with the highest contents of structural intrinsic disorder cluster together in many different eukaryotic interactomes and this is not the case for the prokaryotic E. coli, where proteins with high degree of intrinsic disorder are scarce. I also found that the normalized theta variable from the Popularity-Similarity model for orthologues proteins correlate to the complexity of the organisms in analysis.
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来源期刊
ACS Applied Bio Materials
ACS Applied Bio Materials Chemistry-Chemistry (all)
CiteScore
9.40
自引率
2.10%
发文量
464
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