Optimized Reverse Micelle Surfactant System for High-Resolution NMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolved in Low Viscosity Fluids
journal contributionposted on 17.12.2015, 00:52 by Igor Dodevski, Nathaniel V. Nucci, Kathleen G. Valentine, Gurnimrat K. Sidhu, Evan S. O’Brien, Arthur Pardi, A. Joshua Wand
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.
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Micelle Surfactant Systemreorientation timeEncapsulated Proteinsacidencapsulated macromoleculesviscosity pentanesystems showsolution NMR studiessurfactant systemencapsulated proteinsNucleic Acids Dissolvedchemical shift analysesLow Viscosity FluidsAn optimizedresonance studiesNMR performancemicelle surfactant systemultralow viscosityviscosity fluidsMAGencapsulation conditions