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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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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 |
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author | Kim, Do-Hyoung Lee, Jongchan Mok, K. H. Lee, Jung Ho Han, Kyou-Hoon |
author_facet | Kim, Do-Hyoung Lee, Jongchan Mok, K. H. Lee, Jung Ho Han, Kyou-Hoon |
author_sort | Kim, Do-Hyoung |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7175124 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-71751242020-04-28 Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy Kim, Do-Hyoung Lee, Jongchan Mok, K. H. Lee, Jung Ho Han, Kyou-Hoon Biomolecules Review 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. MDPI 2020-03-10 /pmc/articles/PMC7175124/ /pubmed/32164323 http://dx.doi.org/10.3390/biom10030428 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Kim, Do-Hyoung Lee, Jongchan Mok, K. H. Lee, Jung Ho Han, Kyou-Hoon Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy |
title | Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy |
title_full | Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy |
title_fullStr | Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy |
title_full_unstemmed | Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy |
title_short | Salient Features of Monomeric Alpha-Synuclein Revealed by NMR Spectroscopy |
title_sort | salient features of monomeric alpha-synuclein revealed by nmr spectroscopy |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7175124/ https://www.ncbi.nlm.nih.gov/pubmed/32164323 http://dx.doi.org/10.3390/biom10030428 |
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