{"title":"用NOESY核磁共振研究革兰西菌素在SDS胶束中的阳离子结合定位和氢交换位点","authors":"J.F. Hinton","doi":"10.1006/jmrb.1996.0105","DOIUrl":null,"url":null,"abstract":"<div><p>The site of monovalent cation binding and sites of hydrogen exchange between amide protons and water molecules in the gramicidin A and Phe-1 gramicidin A channels incorporated into SDS micelles have been determined using a NOESY NMR technique. The cation-binding pocket was found to involve residues 10–15 of the peptide.</p></div>","PeriodicalId":16130,"journal":{"name":"Journal of Magnetic Resonance, Series B","volume":"112 1","pages":"Pages 26-31"},"PeriodicalIF":0.0000,"publicationDate":"1996-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/jmrb.1996.0105","citationCount":"6","resultStr":"{\"title\":\"Cation-Binding Location and Hydrogen-Exchange Sites for Gramicidin in SDS Micelles Using NOESY NMR\",\"authors\":\"J.F. Hinton\",\"doi\":\"10.1006/jmrb.1996.0105\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The site of monovalent cation binding and sites of hydrogen exchange between amide protons and water molecules in the gramicidin A and Phe-1 gramicidin A channels incorporated into SDS micelles have been determined using a NOESY NMR technique. The cation-binding pocket was found to involve residues 10–15 of the peptide.</p></div>\",\"PeriodicalId\":16130,\"journal\":{\"name\":\"Journal of Magnetic Resonance, Series B\",\"volume\":\"112 1\",\"pages\":\"Pages 26-31\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1996-07-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1006/jmrb.1996.0105\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Magnetic Resonance, Series B\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1064186696901053\",\"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 Magnetic Resonance, Series B","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1064186696901053","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Cation-Binding Location and Hydrogen-Exchange Sites for Gramicidin in SDS Micelles Using NOESY NMR
The site of monovalent cation binding and sites of hydrogen exchange between amide protons and water molecules in the gramicidin A and Phe-1 gramicidin A channels incorporated into SDS micelles have been determined using a NOESY NMR technique. The cation-binding pocket was found to involve residues 10–15 of the peptide.
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