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dc.contributor.author Kim, Jin Hae -
dc.date.accessioned 2022-07-06T02:33:34Z -
dc.date.available 2022-07-06T02:33:34Z -
dc.date.created 2022-03-28 -
dc.date.issued 2022-03 -
dc.identifier.issn 1226-6531 -
dc.identifier.uri http://hdl.handle.net/20.500.11750/16507 -
dc.description.abstract High-pressure (HP) NMR is a versatile tool to investigate diverse features of proteins. This technique has been particularly powerful to elucidate structural dynamics that only populates sufficiently in a pressurized condition. Amyloidogenic proteins, which are prone to aggregate and form amyloid fibrils, often maintains highly dynamic states in its native or aggregation-prone states, and HP NMR contributed much to advance our understandings of the dynamic behaviors of amyloidogenic proteins and the molecular mechanisms of their aggregation. In this mini review, we therefore summarize recent HP NMR studies on amyloid-beta (Aβ), the representative amyloidogenic intrinsically disordered protein (IDP). -
dc.language English -
dc.publisher Korean Magnetic Resonance Society -
dc.title High-pressure NMR application for amyloid-beta peptides -
dc.type Article -
dc.identifier.doi 10.6564/JKMRS.2022.26.1.017 -
dc.identifier.bibliographicCitation Journal of the Korean Magnetic Resonance Society, v.26, no.1, pp.17 - 20 -
dc.identifier.kciid ART002821098 -
dc.description.isOpenAccess FALSE -
dc.subject.keywordAuthor protein dynamics -
dc.subject.keywordAuthor NMR spectroscopy -
dc.subject.keywordAuthor high-pressure NMR -
dc.subject.keywordAuthor amyloid-beta -
dc.subject.keywordAuthor protein aggregation -
dc.citation.endPage 20 -
dc.citation.number 1 -
dc.citation.startPage 17 -
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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