{"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}
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.