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DC Field Value Language Kim, Bokyung - Kim, Jin Hae - 2021-08-17T20:05:02Z - 2021-08-17T20:05:02Z - 2021-03-25 - 2021-03 -
dc.identifier.issn 1226-6531 -
dc.identifier.uri -
dc.description.abstract Transthyretin (TTR) is an important transporter protein for thyroxine (T4) and a holo-retinol protein in human. In its native state, TTR forms a tetrameric complex to construct the hydrophobic binding pocket for T4. On the other hand, this protein is also infamous for its amyloidogenic propensity, which causes various human diseases, such as senile systemic amyloidosis and familial amyloid polyneuropathy/cardiomyopathy. In this work, to investigate various structural features of TTR with solution-state nuclear magnetic resonance (NMR) spectroscopy, we conducted backbone NMR signal assignments. Except the N-terminal two residues and prolines, backbone 1H-15N signals of all residues were successfully assigned with additional chemical shift information of 13CO, 13Cα, and 13Cβ for most residues. The chemical shift information reported here will become an important basis for subsequent structural and functional studies of TTR. -
dc.language English -
dc.publisher 한국자기공명학회 -
dc.title Backbone NMR chemical shift assignment of transthyretin -
dc.type Article -
dc.identifier.doi 10.6564/JKMRS.2021.25.1.008 -
dc.identifier.bibliographicCitation Journal of the Korean Magnetic Resonance Society, v.25, no.1, pp.8 - 11 -
dc.identifier.kciid ART002695242 -
dc.description.isOpenAccess FALSE -
dc.subject.keywordAuthor transthyretin -
dc.subject.keywordAuthor transthyretin amyloidosis -
dc.subject.keywordAuthor NMR spectroscopy -
dc.subject.keywordAuthor chemical shift assignment -
dc.subject.keywordPlus PRE-ALBUMIN -
dc.subject.keywordPlus PROTEIN -
dc.subject.keywordPlus FIBRIL -
dc.citation.endPage 11 -
dc.citation.number 1 -
dc.citation.startPage 8 -
dc.citation.title Journal of the Korean Magnetic Resonance Society -
dc.citation.volume 25 -
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Department of New Biology Protein Structure Aging Laboratory 1. Journal Articles


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