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dc.contributor.author 김진해 -
dc.date.accessioned 2023-01-10T09:40:10Z -
dc.date.available 2023-01-10T09:40:10Z -
dc.date.created 2022-06-29 -
dc.date.issued 2022-06 -
dc.identifier.issn 1226-6531 -
dc.identifier.uri http://hdl.handle.net/20.500.11750/17354 -
dc.description.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. -
dc.language English -
dc.publisher 한국자기공명학회 -
dc.title High-pressure NMR application for α-synuclein -
dc.title.alternative High-pressure NMR application for α-synuclein -
dc.type Article -
dc.identifier.doi 10.6564/JKMRS.2022.26.2.021 -
dc.identifier.bibliographicCitation Journal of the Korean Magnetic Resonance Society, v.26, no.2, pp.21 - 23 -
dc.identifier.kciid ART002847882 -
dc.description.isOpenAccess FALSE -
dc.subject.keywordAuthor high-pressure NMR -
dc.subject.keywordAuthor α-Synuclein -
dc.subject.keywordAuthor amyloid -
dc.subject.keywordAuthor protein aggregation -
dc.subject.keywordAuthor NMR spectroscopy -
dc.subject.keywordPlus AMYLOID FIBRILS -
dc.subject.keywordPlus DISSOCIATION -
dc.subject.keywordPlus AGGREGATION -
dc.subject.keywordPlus REVEALS -
dc.citation.endPage 23 -
dc.citation.number 2 -
dc.citation.startPage 21 -
dc.citation.title Journal of the Korean Magnetic Resonance Society -
dc.citation.volume 26 -
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Department of New Biology Protein Structure Aging Laboratory 1. Journal Articles

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