Cited 0 time in
Cited 0 time in
Backbone NMR chemical shift assignment of transthyretin
- Title
- Backbone NMR chemical shift assignment of transthyretin
- Authors
- Kim, Bokyung; Kim, 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
- transthyretin; transthyretin amyloidosis; NMR spectroscopy; chemical 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
-
-
Kim, Jin Hae
Protein Structure Aging Laboratory
-
Research Interests
- Files:
There are no files associated with this item.
- Collection:
- Department of New BiologyProtein Structure Aging Laboratory1. Journal Articles
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.