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Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs
Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, allowing determination of oligomeric states o...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Royal Society of Chemistry
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6289172/ https://www.ncbi.nlm.nih.gov/pubmed/30452022 http://dx.doi.org/10.1039/c8cc06284f |
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author | Hellwig, Nils Peetz, Oliver Ahdash, Zainab Tascón, Igor Booth, Paula J. Mikusevic, Vedrana Diskowski, Marina Politis, Argyris Hellmich, Yvonne Hänelt, Inga Reading, Eamonn Morgner, Nina |
author_facet | Hellwig, Nils Peetz, Oliver Ahdash, Zainab Tascón, Igor Booth, Paula J. Mikusevic, Vedrana Diskowski, Marina Politis, Argyris Hellmich, Yvonne Hänelt, Inga Reading, Eamonn Morgner, Nina |
author_sort | Hellwig, Nils |
collection | PubMed |
description | Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, allowing determination of oligomeric states of membrane proteins of different functionality directly from the native nanodiscs. |
format | Online Article Text |
id | pubmed-6289172 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-62891722019-01-09 Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs Hellwig, Nils Peetz, Oliver Ahdash, Zainab Tascón, Igor Booth, Paula J. Mikusevic, Vedrana Diskowski, Marina Politis, Argyris Hellmich, Yvonne Hänelt, Inga Reading, Eamonn Morgner, Nina Chem Commun (Camb) Chemistry Other than more widely used methods, the use of styrene maleic acid allows the direct extraction of membrane proteins from the lipid bilayer into SMALPs keeping it in its native lipid surrounding. Here we present the combined use of SMALPs and LILBID-MS, allowing determination of oligomeric states of membrane proteins of different functionality directly from the native nanodiscs. Royal Society of Chemistry 2018-12-18 2018-11-19 /pmc/articles/PMC6289172/ /pubmed/30452022 http://dx.doi.org/10.1039/c8cc06284f Text en This journal is © The Royal Society of Chemistry 2018 http://creativecommons.org/licenses/by/3.0/ This article is freely available. This article is licensed under a Creative Commons Attribution 3.0 Unported Licence (CC BY 3.0) |
spellingShingle | Chemistry Hellwig, Nils Peetz, Oliver Ahdash, Zainab Tascón, Igor Booth, Paula J. Mikusevic, Vedrana Diskowski, Marina Politis, Argyris Hellmich, Yvonne Hänelt, Inga Reading, Eamonn Morgner, Nina Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs |
title | Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs
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title_full | Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs
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title_fullStr | Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs
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title_full_unstemmed | Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs
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title_short | Native mass spectrometry goes more native: investigation of membrane protein complexes directly from SMALPs
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title_sort | native mass spectrometry goes more native: investigation of membrane protein complexes directly from smalps |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6289172/ https://www.ncbi.nlm.nih.gov/pubmed/30452022 http://dx.doi.org/10.1039/c8cc06284f |
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