[KSCI] Korea Science Citation Index Service

http://dx.doi.org/10.6564/JKMRS.2022.26.2.021

High-pressure NMR application for α-synuclein

Kim, Jin Hae (Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology (DGIST))

Publication Information

Journal of the Korean Magnetic Resonance Society / v.26, no.2, 2022 , pp. 21-23 More about this Journal

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.

Keywords

high-pressure NMR; ${\alpha}-Synuclein$ ; amyloid; protein aggregation; NMR spectroscopy;

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