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Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs
Purified integral membrane proteins require amphipathic molecules to maintain their solubility in aqueous solutions. These complexes, in turn, are used in studies to characterise the protein structures by a variety of biophysical and structural techniques, including spectroscopy, crystallography, an...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6175354/ https://www.ncbi.nlm.nih.gov/pubmed/28925040 http://dx.doi.org/10.1002/bip.23067 |
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author | Ireland, Sam M. Sula, Altin Wallace, B.A. |
author_facet | Ireland, Sam M. Sula, Altin Wallace, B.A. |
author_sort | Ireland, Sam M. |
collection | PubMed |
description | Purified integral membrane proteins require amphipathic molecules to maintain their solubility in aqueous solutions. These complexes, in turn, are used in studies to characterise the protein structures by a variety of biophysical and structural techniques, including spectroscopy, crystallography, and cryo‐electron microscopy. Typically the amphilphiles used have been detergent molecules, but more recently they have included amphipols, which are polymers of different sizes and compositions designed to create smaller, more well‐defined solubilised forms of the membrane proteins. In this study we used circular dichroism spectroscopy to compare the secondary structures and thermal stabilities of the NavMs voltage‐gated sodium channel in different amphipols and detergents as a means of identifying amphipathic environments that maximally maintain the protein structure whilst providing a stabilising environment. These types of characterisations also have potential as means of screening for sample types that may be more suitable for crystallisation and/or cryo‐electron microscopy structure determinations. |
format | Online Article Text |
id | pubmed-6175354 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-61753542018-10-19 Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs Ireland, Sam M. Sula, Altin Wallace, B.A. Biopolymers Original Articles Purified integral membrane proteins require amphipathic molecules to maintain their solubility in aqueous solutions. These complexes, in turn, are used in studies to characterise the protein structures by a variety of biophysical and structural techniques, including spectroscopy, crystallography, and cryo‐electron microscopy. Typically the amphilphiles used have been detergent molecules, but more recently they have included amphipols, which are polymers of different sizes and compositions designed to create smaller, more well‐defined solubilised forms of the membrane proteins. In this study we used circular dichroism spectroscopy to compare the secondary structures and thermal stabilities of the NavMs voltage‐gated sodium channel in different amphipols and detergents as a means of identifying amphipathic environments that maximally maintain the protein structure whilst providing a stabilising environment. These types of characterisations also have potential as means of screening for sample types that may be more suitable for crystallisation and/or cryo‐electron microscopy structure determinations. John Wiley and Sons Inc. 2017-09-19 2018-08 /pmc/articles/PMC6175354/ /pubmed/28925040 http://dx.doi.org/10.1002/bip.23067 Text en © 2017 The Authors Biopolymers Published by Wiley Periodicals, Inc. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Ireland, Sam M. Sula, Altin Wallace, B.A. Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs |
title | Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs |
title_full | Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs |
title_fullStr | Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs |
title_full_unstemmed | Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs |
title_short | Thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel NavMs |
title_sort | thermal melt circular dichroism spectroscopic studies for identifying stabilising amphipathic molecules for the voltage‐gated sodium channel navms |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6175354/ https://www.ncbi.nlm.nih.gov/pubmed/28925040 http://dx.doi.org/10.1002/bip.23067 |
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