结构化随机结合:蛋白质-蛋白质相互作用的最小模型。

Ling-Nan Zou
{"title":"结构化随机结合:蛋白质-蛋白质相互作用的最小模型。","authors":"Ling-Nan Zou","doi":"10.1101/2025.03.26.645477","DOIUrl":null,"url":null,"abstract":"<p><p>We describe Structured Random Binding (SRB), a minimal model of protein-protein interactions rooted in the statistical physics of disordered systems. In this model, nonspecific binding is a generic consequence of the interaction between random proteins, exhibiting a phase transition from a high temperature state where nonspecific complexes are transient and lack well-defined interaction interfaces, to a low temperature state where the complex structure is frozen and a definite interaction interface is present. Numerically, weakly-bound nonspecific complexes can evolve into tightly-bound, highly specific complexes, but only if the structural correlation length along the peptide backbone is short; moreover, evolved tightly-bound homodimers favor the same interface structure that is predominant in real protein homodimers.</p>","PeriodicalId":519960,"journal":{"name":"bioRxiv : the preprint server for biology","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11974877/pdf/","citationCount":"0","resultStr":"{\"title\":\"Structured Random Binding: a minimal model of protein-protein interactions.\",\"authors\":\"Ling-Nan Zou\",\"doi\":\"10.1101/2025.03.26.645477\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>We describe Structured Random Binding (SRB), a minimal model of protein-protein interactions rooted in the statistical physics of disordered systems. In this model, nonspecific binding is a generic consequence of the interaction between random proteins, exhibiting a phase transition from a high temperature state where nonspecific complexes are transient and lack well-defined interaction interfaces, to a low temperature state where the complex structure is frozen and a definite interaction interface is present. Numerically, weakly-bound nonspecific complexes can evolve into tightly-bound, highly specific complexes, but only if the structural correlation length along the peptide backbone is short; moreover, evolved tightly-bound homodimers favor the same interface structure that is predominant in real protein homodimers.</p>\",\"PeriodicalId\":519960,\"journal\":{\"name\":\"bioRxiv : the preprint server for biology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-03-29\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11974877/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"bioRxiv : the preprint server for biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1101/2025.03.26.645477\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"bioRxiv : the preprint server for biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1101/2025.03.26.645477","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

我们描述了结构化随机结合(SRB),这是一个基于无序系统统计物理的蛋白质-蛋白质相互作用的最小模型。在该模型中,非特异性结合是随机蛋白质之间相互作用的一般结果,表现出从高温状态到低温状态的相变,在高温状态下,非特异性复合物是短暂的,缺乏明确的相互作用界面,在低温状态下,复杂结构被冻结,存在明确的相互作用界面。数值上,弱结合的非特异性配合物可以进化成紧密结合的高特异性配合物,但前提是肽主链上的结构相关长度较短;此外,进化的紧密结合的同型二聚体支持与真正的蛋白质同型二聚体相同的界面结构。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structured Random Binding: a minimal model of protein-protein interactions.

We describe Structured Random Binding (SRB), a minimal model of protein-protein interactions rooted in the statistical physics of disordered systems. In this model, nonspecific binding is a generic consequence of the interaction between random proteins, exhibiting a phase transition from a high temperature state where nonspecific complexes are transient and lack well-defined interaction interfaces, to a low temperature state where the complex structure is frozen and a definite interaction interface is present. Numerically, weakly-bound nonspecific complexes can evolve into tightly-bound, highly specific complexes, but only if the structural correlation length along the peptide backbone is short; moreover, evolved tightly-bound homodimers favor the same interface structure that is predominant in real protein homodimers.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信