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Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR
Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a near...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8580007/ https://www.ncbi.nlm.nih.gov/pubmed/34880983 http://dx.doi.org/10.1039/d1sc02813h |
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author | Xue, Kai Movellan, Kumar Tekwani Zhang, Xizhou Cecily Najbauer, Eszter E. Forster, Marcel C. Becker, Stefan Andreas, Loren B. |
author_facet | Xue, Kai Movellan, Kumar Tekwani Zhang, Xizhou Cecily Najbauer, Eszter E. Forster, Marcel C. Becker, Stefan Andreas, Loren B. |
author_sort | Xue, Kai |
collection | PubMed |
description | Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a near-native lipid bilayer environment. The main limitation of the method is spectral resolution and sensitivity, however recent developments in ssNMR hardware, including the commercialization of 28 T magnets (1.2 GHz proton frequency) and ultrafast MAS spinning (<100 kHz) promise to accelerate acquisition, while reducing sample requirement, both of which are critical to membrane protein studies. Here, we review recent advances in ssNMR methodology used for structure determination of membrane proteins in native and mimetic environments, as well as the study of protein functions such as protein dynamics, and interactions with ligands, lipids and cholesterol. |
format | Online Article Text |
id | pubmed-8580007 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-85800072021-12-07 Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR Xue, Kai Movellan, Kumar Tekwani Zhang, Xizhou Cecily Najbauer, Eszter E. Forster, Marcel C. Becker, Stefan Andreas, Loren B. Chem Sci Chemistry Solid-state NMR (ssNMR) is a versatile technique that can be used for the characterization of various materials, ranging from small molecules to biological samples, including membrane proteins. ssNMR can probe both the structure and dynamics of membrane proteins, revealing protein function in a near-native lipid bilayer environment. The main limitation of the method is spectral resolution and sensitivity, however recent developments in ssNMR hardware, including the commercialization of 28 T magnets (1.2 GHz proton frequency) and ultrafast MAS spinning (<100 kHz) promise to accelerate acquisition, while reducing sample requirement, both of which are critical to membrane protein studies. Here, we review recent advances in ssNMR methodology used for structure determination of membrane proteins in native and mimetic environments, as well as the study of protein functions such as protein dynamics, and interactions with ligands, lipids and cholesterol. The Royal Society of Chemistry 2021-09-07 /pmc/articles/PMC8580007/ /pubmed/34880983 http://dx.doi.org/10.1039/d1sc02813h Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Xue, Kai Movellan, Kumar Tekwani Zhang, Xizhou Cecily Najbauer, Eszter E. Forster, Marcel C. Becker, Stefan Andreas, Loren B. Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR |
title | Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR |
title_full | Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR |
title_fullStr | Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR |
title_full_unstemmed | Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR |
title_short | Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR |
title_sort | towards a native environment: structure and function of membrane proteins in lipid bilayers by nmr |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8580007/ https://www.ncbi.nlm.nih.gov/pubmed/34880983 http://dx.doi.org/10.1039/d1sc02813h |
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