{"title":"超过20,000 M(r)的蛋白质和蛋白质复合物的核磁共振结构。","authors":"G M Clore, A M Gronenborn","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.</p>","PeriodicalId":18848,"journal":{"name":"Nature Structural Biology","volume":"4 Suppl ","pages":"849-53"},"PeriodicalIF":0.0000,"publicationDate":"1997-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"NMR structures of proteins and protein complexes beyond 20,000 M(r).\",\"authors\":\"G M Clore, A M Gronenborn\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.</p>\",\"PeriodicalId\":18848,\"journal\":{\"name\":\"Nature Structural Biology\",\"volume\":\"4 Suppl \",\"pages\":\"849-53\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1997-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Structural Biology\",\"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":"Nature Structural Biology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
NMR structures of proteins and protein complexes beyond 20,000 M(r).
Recent advances in multidimensional NMR to obtain resonance assignments, interproton distance and torsion angle restraints, and restraints that characterize long range order, coupled with new methods of structure refinement, have permitted solution structures of proteins in excess of 250 residues to be solved.