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Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
[Image: see text] An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids. Comprising the nonionic 1-decanoyl-rac-glycerol and the zwitterionic lauryldimethylamine-N...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3969725/ https://www.ncbi.nlm.nih.gov/pubmed/24495164 http://dx.doi.org/10.1021/ja410716w |
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author | Dodevski, Igor Nucci, Nathaniel V. Valentine, Kathleen G. Sidhu, Gurnimrat K. O’Brien, Evan S. Pardi, Arthur Wand, A. Joshua |
author_facet | Dodevski, Igor Nucci, Nathaniel V. Valentine, Kathleen G. Sidhu, Gurnimrat K. O’Brien, Evan S. Pardi, Arthur Wand, A. Joshua |
author_sort | Dodevski, Igor |
collection | PubMed |
description | [Image: see text] An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids. Comprising the nonionic 1-decanoyl-rac-glycerol and the zwitterionic lauryldimethylamine-N-oxide (10MAG/LDAO), this mixture is shown to efficiently encapsulate a diverse set of proteins and nucleic acids. Chemical shift analyses of these systems show that high structural fidelity is achieved upon encapsulation. The 10MAG/LDAO surfactant system reduces the molecular reorientation time for encapsulated macromolecules larger than ∼20 kDa leading to improved overall NMR performance. The 10MAG/LDAO system can also be used for solution NMR studies of lipid-modified proteins. New and efficient strategies for optimization of encapsulation conditions are described. 10MAG/LDAO performs well in both the low viscosity pentane and ultralow viscosity liquid ethane and therefore will serve as a general surfactant system for initiating solution NMR studies of proteins and nucleic acids. |
format | Online Article Text |
id | pubmed-3969725 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-39697252015-02-04 Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids Dodevski, Igor Nucci, Nathaniel V. Valentine, Kathleen G. Sidhu, Gurnimrat K. O’Brien, Evan S. Pardi, Arthur Wand, A. Joshua J Am Chem Soc [Image: see text] An optimized reverse micelle surfactant system has been developed for solution nuclear magnetic resonance studies of encapsulated proteins and nucleic acids dissolved in low viscosity fluids. Comprising the nonionic 1-decanoyl-rac-glycerol and the zwitterionic lauryldimethylamine-N-oxide (10MAG/LDAO), this mixture is shown to efficiently encapsulate a diverse set of proteins and nucleic acids. Chemical shift analyses of these systems show that high structural fidelity is achieved upon encapsulation. The 10MAG/LDAO surfactant system reduces the molecular reorientation time for encapsulated macromolecules larger than ∼20 kDa leading to improved overall NMR performance. The 10MAG/LDAO system can also be used for solution NMR studies of lipid-modified proteins. New and efficient strategies for optimization of encapsulation conditions are described. 10MAG/LDAO performs well in both the low viscosity pentane and ultralow viscosity liquid ethane and therefore will serve as a general surfactant system for initiating solution NMR studies of proteins and nucleic acids. American Chemical Society 2014-02-04 2014-03-05 /pmc/articles/PMC3969725/ /pubmed/24495164 http://dx.doi.org/10.1021/ja410716w Text en Copyright © 2014 American Chemical Society |
spellingShingle | Dodevski, Igor Nucci, Nathaniel V. Valentine, Kathleen G. Sidhu, Gurnimrat K. O’Brien, Evan S. Pardi, Arthur Wand, A. Joshua Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids |
title | Optimized
Reverse Micelle Surfactant System for High-Resolution
NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved
in Low Viscosity Fluids |
title_full | Optimized
Reverse Micelle Surfactant System for High-Resolution
NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved
in Low Viscosity Fluids |
title_fullStr | Optimized
Reverse Micelle Surfactant System for High-Resolution
NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved
in Low Viscosity Fluids |
title_full_unstemmed | Optimized
Reverse Micelle Surfactant System for High-Resolution
NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved
in Low Viscosity Fluids |
title_short | Optimized
Reverse Micelle Surfactant System for High-Resolution
NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved
in Low Viscosity Fluids |
title_sort | optimized
reverse micelle surfactant system for high-resolution
nmr spectroscopy of encapsulated proteins and nucleic acids dissolved
in low viscosity fluids |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3969725/ https://www.ncbi.nlm.nih.gov/pubmed/24495164 http://dx.doi.org/10.1021/ja410716w |
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