确定迁移率(刚性)与界面残馀守恒之间的对应关系

Gozde Kar, A. Gursoy, O. Keskin
{"title":"确定迁移率(刚性)与界面残馀守恒之间的对应关系","authors":"Gozde Kar, A. Gursoy, O. Keskin","doi":"10.1109/HIBIT.2010.5478887","DOIUrl":null,"url":null,"abstract":"Hot spots at protein interfaces may play specific functional roles and contribute to the stability of the protein complex. These residues are not homogeneously distributed along the protein interfaces; rather they are clustered within locally tightly packed regions forming a network of interactions among themselves. Here, we investigate the organization of computational hot spots at protein interfaces. A list of proteins whose free and bound forms exist is examined. Inter-residue distances of the interface residues are compared for both forms. Results reveal that there exist rigid block regions at protein interfaces. More interestingly, these regions correspond to computational hot regions. Hot spots can be determined with an average positive predictive value (PPV) of 0.73 and average sensitivity value of 0.70 for seven protein complexes.","PeriodicalId":215457,"journal":{"name":"2010 5th International Symposium on Health Informatics and Bioinformatics","volume":"15 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2010-04-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Determination of the correspondence between mobility (rigidity) and conservation of the interface residues\",\"authors\":\"Gozde Kar, A. Gursoy, O. Keskin\",\"doi\":\"10.1109/HIBIT.2010.5478887\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Hot spots at protein interfaces may play specific functional roles and contribute to the stability of the protein complex. These residues are not homogeneously distributed along the protein interfaces; rather they are clustered within locally tightly packed regions forming a network of interactions among themselves. Here, we investigate the organization of computational hot spots at protein interfaces. A list of proteins whose free and bound forms exist is examined. Inter-residue distances of the interface residues are compared for both forms. Results reveal that there exist rigid block regions at protein interfaces. More interestingly, these regions correspond to computational hot regions. Hot spots can be determined with an average positive predictive value (PPV) of 0.73 and average sensitivity value of 0.70 for seven protein complexes.\",\"PeriodicalId\":215457,\"journal\":{\"name\":\"2010 5th International Symposium on Health Informatics and Bioinformatics\",\"volume\":\"15 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2010-04-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"2010 5th International Symposium on Health Informatics and Bioinformatics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1109/HIBIT.2010.5478887\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"2010 5th International Symposium on Health Informatics and Bioinformatics","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/HIBIT.2010.5478887","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

蛋白质界面上的热点可能起着特定的功能作用,并有助于蛋白质复合物的稳定性。这些残基沿蛋白质界面分布不均匀;相反,它们聚集在局部紧密排列的区域内,形成相互作用的网络。在这里,我们研究了蛋白质界面上计算热点的组织。检查了自由形式和结合形式存在的蛋白质列表。比较了两种形式的界面残基间残基距离。结果表明,在蛋白质界面处存在刚性块区。更有趣的是,这些区域对应于计算热点区域。7种蛋白复合物的平均阳性预测值(PPV)为0.73,平均敏感性值为0.70。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Determination of the correspondence between mobility (rigidity) and conservation of the interface residues
Hot spots at protein interfaces may play specific functional roles and contribute to the stability of the protein complex. These residues are not homogeneously distributed along the protein interfaces; rather they are clustered within locally tightly packed regions forming a network of interactions among themselves. Here, we investigate the organization of computational hot spots at protein interfaces. A list of proteins whose free and bound forms exist is examined. Inter-residue distances of the interface residues are compared for both forms. Results reveal that there exist rigid block regions at protein interfaces. More interestingly, these regions correspond to computational hot regions. Hot spots can be determined with an average positive predictive value (PPV) of 0.73 and average sensitivity value of 0.70 for seven protein complexes.
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:604180095
Book学术官方微信