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Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy

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...

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Detalles Bibliográficos
Autores principales: Kim, Do-Hyoung, Lee, Jongchan, Mok, K. H., Lee, Jung Ho, Han, Kyou-Hoon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7175124/
https://www.ncbi.nlm.nih.gov/pubmed/32164323
http://dx.doi.org/10.3390/biom10030428
Descripción
Sumario: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.