{"title":"RRM设计/spl α /-凝乳胰蛋白酶样肽","authors":"E. Lazoura, I. Cosic","doi":"10.1109/ICBEM.1998.666411","DOIUrl":null,"url":null,"abstract":"The Resonant Recognition Model (RRM) has been applied to chymotrypsin to design peptides that exhibit chymotrypsin-like activity. Molecular modelling studies indicate that a 19-mer (chlida 2), which has a f/sub RRM/=0.2344 and /spl phi/=-1.186, folds appropriately so that the spatial separation of the amino acids required for chymotrypsin activity is comparable with that of /spl alpha/-chymotrypsin.","PeriodicalId":213764,"journal":{"name":"Proceedings of the 2nd International Conference on Bioelectromagnetism (Cat. No.98TH8269)","volume":"8 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"1998-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"RRM designed /spl alpha/-chymotrypsin-like peptides\",\"authors\":\"E. Lazoura, I. Cosic\",\"doi\":\"10.1109/ICBEM.1998.666411\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The Resonant Recognition Model (RRM) has been applied to chymotrypsin to design peptides that exhibit chymotrypsin-like activity. Molecular modelling studies indicate that a 19-mer (chlida 2), which has a f/sub RRM/=0.2344 and /spl phi/=-1.186, folds appropriately so that the spatial separation of the amino acids required for chymotrypsin activity is comparable with that of /spl alpha/-chymotrypsin.\",\"PeriodicalId\":213764,\"journal\":{\"name\":\"Proceedings of the 2nd International Conference on Bioelectromagnetism (Cat. No.98TH8269)\",\"volume\":\"8 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1998-02-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Proceedings of the 2nd International Conference on Bioelectromagnetism (Cat. No.98TH8269)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1109/ICBEM.1998.666411\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Proceedings of the 2nd International Conference on Bioelectromagnetism (Cat. No.98TH8269)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1109/ICBEM.1998.666411","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
RRM designed /spl alpha/-chymotrypsin-like peptides
The Resonant Recognition Model (RRM) has been applied to chymotrypsin to design peptides that exhibit chymotrypsin-like activity. Molecular modelling studies indicate that a 19-mer (chlida 2), which has a f/sub RRM/=0.2344 and /spl phi/=-1.186, folds appropriately so that the spatial separation of the amino acids required for chymotrypsin activity is comparable with that of /spl alpha/-chymotrypsin.
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