{"title":"利用同位素标记对较大的蛋白质进行核磁共振研究","authors":"Sung Jean Park","doi":"10.6564/JKMRS.2014.18.2.047","DOIUrl":null,"url":null,"abstract":"Larger proteins (above molecular weight 50 kDa) usually show slow motional tumbling in solution, which facilitates the decay of NMR signal, resulting in poor signal-to-noise. In the past twenty years, researchers have tried to overcome this problem with higher molecular weight by improvement of hardware (higher magnetic field and cryoprobe), optimization of pulse sequences for lager molecules, and development of isotope-labeling techniques. Actually, GroEL/ES complex (≈ 900 kDa) was successfully studied using combination of above techniques. Among the techniques used in large molecular studies, the impact of isotope-labeling for large molecules study is summarized and discussed here.","PeriodicalId":17414,"journal":{"name":"Journal of the Korean magnetic resonance society","volume":"9 1","pages":"47-51"},"PeriodicalIF":0.4000,"publicationDate":"2014-12-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"6","resultStr":"{\"title\":\"NMR Study of larger proteins using isotope labeling\",\"authors\":\"Sung Jean Park\",\"doi\":\"10.6564/JKMRS.2014.18.2.047\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Larger proteins (above molecular weight 50 kDa) usually show slow motional tumbling in solution, which facilitates the decay of NMR signal, resulting in poor signal-to-noise. In the past twenty years, researchers have tried to overcome this problem with higher molecular weight by improvement of hardware (higher magnetic field and cryoprobe), optimization of pulse sequences for lager molecules, and development of isotope-labeling techniques. Actually, GroEL/ES complex (≈ 900 kDa) was successfully studied using combination of above techniques. Among the techniques used in large molecular studies, the impact of isotope-labeling for large molecules study is summarized and discussed here.\",\"PeriodicalId\":17414,\"journal\":{\"name\":\"Journal of the Korean magnetic resonance society\",\"volume\":\"9 1\",\"pages\":\"47-51\"},\"PeriodicalIF\":0.4000,\"publicationDate\":\"2014-12-20\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the Korean magnetic resonance society\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.6564/JKMRS.2014.18.2.047\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOCHEMICAL RESEARCH METHODS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Korean magnetic resonance society","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.6564/JKMRS.2014.18.2.047","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMICAL RESEARCH METHODS","Score":null,"Total":0}
NMR Study of larger proteins using isotope labeling
Larger proteins (above molecular weight 50 kDa) usually show slow motional tumbling in solution, which facilitates the decay of NMR signal, resulting in poor signal-to-noise. In the past twenty years, researchers have tried to overcome this problem with higher molecular weight by improvement of hardware (higher magnetic field and cryoprobe), optimization of pulse sequences for lager molecules, and development of isotope-labeling techniques. Actually, GroEL/ES complex (≈ 900 kDa) was successfully studied using combination of above techniques. Among the techniques used in large molecular studies, the impact of isotope-labeling for large molecules study is summarized and discussed here.