{"title":"埃博拉病毒糖蛋白受体结合域的多因子分析","authors":"J. Weltman","doi":"10.4172/2161-0703.1000217","DOIUrl":null,"url":null,"abstract":"An analysis of the receptor-binding domain (RBD) of the ZEBOV-Makona glycoprotein is presented, based upon the following four factors: information entropy (H), protein conformation, thermal imprint (B factor) and predicted epitope activity (Bepipred Score). It was found that the position of maximum information entropy (Hmax) was located within a helical pentapeptide component of a 31-mer peptide in which H=0 at each amino acid except at the amino acid position where H=Hmax. It is proposed that identification of these RBD peptide components and characteristics can help facilitate efficient design of an anti-Ebola vaccine.","PeriodicalId":269971,"journal":{"name":"Journal of Medical Microbiology and Diagnosis","volume":"33 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2016-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"A Multifactorial Analysis of Ebola Virus Glycoprotein Receptor BindingDomain\",\"authors\":\"J. Weltman\",\"doi\":\"10.4172/2161-0703.1000217\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"An analysis of the receptor-binding domain (RBD) of the ZEBOV-Makona glycoprotein is presented, based upon the following four factors: information entropy (H), protein conformation, thermal imprint (B factor) and predicted epitope activity (Bepipred Score). It was found that the position of maximum information entropy (Hmax) was located within a helical pentapeptide component of a 31-mer peptide in which H=0 at each amino acid except at the amino acid position where H=Hmax. It is proposed that identification of these RBD peptide components and characteristics can help facilitate efficient design of an anti-Ebola vaccine.\",\"PeriodicalId\":269971,\"journal\":{\"name\":\"Journal of Medical Microbiology and Diagnosis\",\"volume\":\"33 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2016-02-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Medical Microbiology and Diagnosis\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.4172/2161-0703.1000217\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Medical Microbiology and Diagnosis","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.4172/2161-0703.1000217","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
A Multifactorial Analysis of Ebola Virus Glycoprotein Receptor BindingDomain
An analysis of the receptor-binding domain (RBD) of the ZEBOV-Makona glycoprotein is presented, based upon the following four factors: information entropy (H), protein conformation, thermal imprint (B factor) and predicted epitope activity (Bepipred Score). It was found that the position of maximum information entropy (Hmax) was located within a helical pentapeptide component of a 31-mer peptide in which H=0 at each amino acid except at the amino acid position where H=Hmax. It is proposed that identification of these RBD peptide components and characteristics can help facilitate efficient design of an anti-Ebola vaccine.
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