{"title":"无序中的联系:非原生相互作用可能支持蛋白质的远程偶联。","authors":"Hue Sun Chan, Zhuqing Zhang","doi":"10.1186/jbiol126","DOIUrl":null,"url":null,"abstract":"<p><p>A lattice-model study of double-mutant cycles published in BMC Structural Biology underscores how interactions in non-native conformations can lead to thermodynamic coupling between distant residues in globular proteins, adding to recent advances in delineating the often crucial roles played by disordered conformational ensembles in protein behavior.</p>","PeriodicalId":15075,"journal":{"name":"Journal of Biology","volume":"8 3","pages":"27"},"PeriodicalIF":0.0000,"publicationDate":"2009-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/jbiol126","citationCount":"6","resultStr":"{\"title\":\"Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins.\",\"authors\":\"Hue Sun Chan, Zhuqing Zhang\",\"doi\":\"10.1186/jbiol126\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>A lattice-model study of double-mutant cycles published in BMC Structural Biology underscores how interactions in non-native conformations can lead to thermodynamic coupling between distant residues in globular proteins, adding to recent advances in delineating the often crucial roles played by disordered conformational ensembles in protein behavior.</p>\",\"PeriodicalId\":15075,\"journal\":{\"name\":\"Journal of Biology\",\"volume\":\"8 3\",\"pages\":\"27\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2009-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1186/jbiol126\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Biology\",\"FirstCategoryId\":\"1089\",\"ListUrlMain\":\"https://doi.org/10.1186/jbiol126\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2009/3/13 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Biology","FirstCategoryId":"1089","ListUrlMain":"https://doi.org/10.1186/jbiol126","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2009/3/13 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
Liaison amid disorder: non-native interactions may underpin long-range coupling in proteins.
A lattice-model study of double-mutant cycles published in BMC Structural Biology underscores how interactions in non-native conformations can lead to thermodynamic coupling between distant residues in globular proteins, adding to recent advances in delineating the often crucial roles played by disordered conformational ensembles in protein behavior.
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