下载PDF
{"title":"利用定位自旋标记(SDSL)测定可溶性蛋白的脉冲EPR距离","authors":"Ian Mitchelle S. de Vera, Mandy E. Blackburn, Luis Galiano, Gail E. Fanucci","doi":"10.1002/0471140864.ps1717s74","DOIUrl":null,"url":null,"abstract":"<p>The resurgence of pulsed electron paramagnetic resonance (EPR) in structural biology centers on recent improvements in distance measurements using the double electron-electron resonance (DEER) technique. This unit focuses on EPR-based distance measurements by site-directed spin labeling (SDSL) of engineered cysteine residues in soluble proteins, with HIV-1 protease used as a model. To elucidate conformational changes in proteins, experimental protocols were optimized and existing data analysis programs were employed to derive distance-distribution profiles. Experimental considerations, sample preparation, and error analysis for artifact suppression are also outlined herein. <i>Curr. Protoc. Protein Sci</i>. 74:17.17.1-17.17.29. © 2013 by John Wiley & Sons, Inc.</p>","PeriodicalId":10866,"journal":{"name":"Current Protocols in Protein Science","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2018-02-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1002/0471140864.ps1717s74","citationCount":"19","resultStr":"{\"title\":\"Pulsed EPR Distance Measurements in Soluble Proteins by Site-Directed Spin Labeling (SDSL)\",\"authors\":\"Ian Mitchelle S. de Vera, Mandy E. Blackburn, Luis Galiano, Gail E. Fanucci\",\"doi\":\"10.1002/0471140864.ps1717s74\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>The resurgence of pulsed electron paramagnetic resonance (EPR) in structural biology centers on recent improvements in distance measurements using the double electron-electron resonance (DEER) technique. This unit focuses on EPR-based distance measurements by site-directed spin labeling (SDSL) of engineered cysteine residues in soluble proteins, with HIV-1 protease used as a model. To elucidate conformational changes in proteins, experimental protocols were optimized and existing data analysis programs were employed to derive distance-distribution profiles. Experimental considerations, sample preparation, and error analysis for artifact suppression are also outlined herein. <i>Curr. Protoc. Protein Sci</i>. 74:17.17.1-17.17.29. © 2013 by John Wiley & Sons, Inc.</p>\",\"PeriodicalId\":10866,\"journal\":{\"name\":\"Current Protocols in Protein Science\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2018-02-16\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1002/0471140864.ps1717s74\",\"citationCount\":\"19\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Current Protocols in Protein Science\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/0471140864.ps1717s74\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"Biochemistry, Genetics and Molecular Biology\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Current Protocols in Protein Science","FirstCategoryId":"1085","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/0471140864.ps1717s74","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 19
引用
批量引用
京公网安备 11010802042870号
京ICP备2023020795号-1
分享
求助内容：
应助结果提醒方式：
扫码关注我们
