Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy
Do-Hyoung Kim, Jong‐Chan Lee, Jong‐Chan Lee, K. Hun Mok, Jung Eun Lee, Jung Eun Lee, Kyou‐Hoon Han
Abstract
Elucidating the structural details of proteins is highly valuable and important for the proper understanding of protein function. In the case of intrinsically disordered proteins (IDPs), however, obtaining the structural details is quite challenging, as the traditional structural biology tools have only limited use. Nuclear magnetic resonance (NMR) is a unique experimental tool that provides ensemble conformations of IDPs at atomic resolution, and when studying IDPs, a slightly different experimental strategy needs to be employed than the one used for globular proteins. We address this point by reviewing many NMR investigations carried out on the α-synuclein protein, the aggregation of which is strongly correlated with Parkinson's disease.