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Backbone NMR chemical shift assignment of transthyretin

Title
Backbone NMR chemical shift assignment of transthyretin
Authors
Kim, BokyungKim, Jin Hae
DGIST Authors
Kim, Bokyung; Kim, Jin Hae
Issue Date
2021-03
Citation
Journal of the Korean Magnetic Resonance Society, 25(1), 8-11
Type
Article
Author Keywords
transthyretintransthyretin amyloidosisNMR spectroscopychemical shift assignment
ISSN
1226-6531
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.
URI
http://hdl.handle.net/20.500.11750/13975
DOI
10.6564/JKMRS.2021.25.1.008
Publisher
한국자기공명학회
Related Researcher
Files:
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Collection:
Department of New BiologyProtein Structure Aging Laboratory1. Journal Articles


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