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NMR Study of larger proteins using isotope labeling

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dc.contributor.author박성진-
dc.date.available2020-02-28T19:44:08Z-
dc.date.created2020-02-12-
dc.date.issued2014-
dc.identifier.issn1226-6531-
dc.identifier.urihttps://scholarworks.bwise.kr/gachon/handle/2020.sw.gachon/13308-
dc.description.abstractLarger 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 techniques1. Among the techniques used in large molecular studies, the impact of isotope-labeling for large molecules study is summarized and discussed here.-
dc.language영어-
dc.language.isoen-
dc.publisher한국자기공명학회-
dc.relation.isPartOfJournal of the Korean Magnetic Resonance Society-
dc.titleNMR Study of larger proteins using isotope labeling-
dc.typeArticle-
dc.type.rimsART-
dc.description.journalClass2-
dc.identifier.doi10.6564/JKMRS.2014.18.2.047-
dc.identifier.bibliographicCitationJournal of the Korean Magnetic Resonance Society, v.18, no.2, pp.47 - 51-
dc.identifier.kciidART001935767-
dc.citation.endPage51-
dc.citation.startPage47-
dc.citation.titleJournal of the Korean Magnetic Resonance Society-
dc.citation.volume18-
dc.citation.number2-
dc.contributor.affiliatedAuthor박성진-
dc.subject.keywordAuthorNMR-
dc.subject.keywordAuthorLarge molecular weight-
dc.subject.keywordAuthorIsotope labeling-
dc.subject.keywordAuthorMethyl TROSY-
dc.description.journalRegisteredClasskci-
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