{"title":"蛋白质紊乱如何将内部动力学转变为远程调节开关","authors":"","doi":"10.1038/s41594-025-01588-4","DOIUrl":null,"url":null,"abstract":"Understanding how proteins are regulated remains a fundamental challenge in molecular biology. Our findings demonstrate how a flexible, disordered protein segment — an intrinsically disordered region — can remotely silence or activate protein function by tuning internal dynamics via an entropy-driven regulatory mechanism without structural change or direct protein contact.","PeriodicalId":18822,"journal":{"name":"Nature structural & molecular biology","volume":"103 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-06-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"How protein disorder turns internal dynamics into a long-range regulatory switch\",\"authors\":\"\",\"doi\":\"10.1038/s41594-025-01588-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Understanding how proteins are regulated remains a fundamental challenge in molecular biology. Our findings demonstrate how a flexible, disordered protein segment — an intrinsically disordered region — can remotely silence or activate protein function by tuning internal dynamics via an entropy-driven regulatory mechanism without structural change or direct protein contact.\",\"PeriodicalId\":18822,\"journal\":{\"name\":\"Nature structural & molecular biology\",\"volume\":\"103 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-06-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature structural & molecular biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1038/s41594-025-01588-4\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature structural & molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1038/s41594-025-01588-4","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
How protein disorder turns internal dynamics into a long-range regulatory switch
Understanding how proteins are regulated remains a fundamental challenge in molecular biology. Our findings demonstrate how a flexible, disordered protein segment — an intrinsically disordered region — can remotely silence or activate protein function by tuning internal dynamics via an entropy-driven regulatory mechanism without structural change or direct protein contact.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
