{"title":"跨膜α -螺旋的结构方面。","authors":"G von Heijne","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Integral membrane proteins have recently moved to center stage in structural biology, partly as a result of the realization that a large number of widely used drugs are targeted to membrane proteins. 3D structure determination of membrane proteins is, however, exceedingly difficult, and alternative means of obtaining structurally relevant information must be sought. In this short communication, a new way to study the conformation and membrane localization of a single transmembrane protein segment--glycosylation mapping--is introduced.</p>","PeriodicalId":75414,"journal":{"name":"Acta physiologica Scandinavica. Supplementum","volume":"643 ","pages":"17-9"},"PeriodicalIF":0.0000,"publicationDate":"1998-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Structural aspects of transmembrane alpha-helices.\",\"authors\":\"G von Heijne\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Integral membrane proteins have recently moved to center stage in structural biology, partly as a result of the realization that a large number of widely used drugs are targeted to membrane proteins. 3D structure determination of membrane proteins is, however, exceedingly difficult, and alternative means of obtaining structurally relevant information must be sought. In this short communication, a new way to study the conformation and membrane localization of a single transmembrane protein segment--glycosylation mapping--is introduced.</p>\",\"PeriodicalId\":75414,\"journal\":{\"name\":\"Acta physiologica Scandinavica. Supplementum\",\"volume\":\"643 \",\"pages\":\"17-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Acta physiologica Scandinavica. Supplementum\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Acta physiologica Scandinavica. Supplementum","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Structural aspects of transmembrane alpha-helices.
Integral membrane proteins have recently moved to center stage in structural biology, partly as a result of the realization that a large number of widely used drugs are targeted to membrane proteins. 3D structure determination of membrane proteins is, however, exceedingly difficult, and alternative means of obtaining structurally relevant information must be sought. In this short communication, a new way to study the conformation and membrane localization of a single transmembrane protein segment--glycosylation mapping--is introduced.