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High-pressure NMR application for α-synuclein

Title
High-pressure NMR application for α-synuclein
Alternative Title
High-pressure NMR application for α-synuclein
Author(s)
김진해
Issued Date
2022-06
Citation
Journal of the Korean Magnetic Resonance Society, v.26, no.2, pp.21 - 23
Type
Article
Author Keywords
high-pressure NMRα-Synucleinamyloidprotein aggregationNMR spectroscopy
Keywords
AMYLOID FIBRILSDISSOCIATIONAGGREGATIONREVEALS
ISSN
1226-6531
Abstract
High-pressure (HP) NMR is a powerful method to elucidate various structural features of amyloidogenic proteins. Following the previous mini-review recapitulating the HP-NMR application for amyloid-β peptides of the last issue [J. H. Kim, J. Kor. Mag. Reson. Soc. 26, 17 (2022)], the recent advancements in the HP NMR application for α-synuclein (α-Syn) are briefly summarized and discussed here. Although α-Syn is a well-known intrinsically disordered protein (IDP), several studies have shown that it can also exhibit heterogeneous yet partially folded conformations, which may correlate with its amyloid-forming propensity. HP NMR has been a valuable tool for investigating the dynamic and transient structural features of α-Syn and has provided unique insights to appreciate its aggregation-prone characters.
URI
http://hdl.handle.net/20.500.11750/17354
DOI
10.6564/JKMRS.2022.26.2.021
Publisher
한국자기공명학회
Related Researcher
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Appears in Collections:
Department of New Biology Protein Structure Aging Laboratory 1. Journal Articles

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