Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
| Autor: | Gurnimrat K. Sidhu, A. Joshua Wand, Arthur Pardi, Igor Dodevski, Nathaniel V. Nucci, Kathleen G. Valentine, Evan S. O'Brien |
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| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Magnetic Resonance Spectroscopy Molecular Conformation Capsules Biochemistry Micelle Article Catalysis Surface-Active Agents Viscosity chemistry.chemical_compound Colloid and Surface Chemistry Spectroscopy Micelles Chromatography Chemistry Membrane Proteins DNA General Chemistry Nuclear magnetic resonance spectroscopy Pentane Membrane protein Chemical engineering Nucleic acid RNA Volatilization Dimethylamines Macromolecule |
| Zdroj: | Journal of the American Chemical Society |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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