투고논문

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, α-Synuclein, amyloid, protein aggregation, NMR spectroscopy

* Address correspondence to: Jin Hae Kim, Department of New Biology, Daegu Gyeongbuk Institute of Science & Technology (DGIST), Daegu 42988, Republic of Korea, Tel: 82-53-785-1770; E-mail: jinhaekim@dgist.ac.kr