[NMR paper] Optimized reverse micelle surfactant system for high-resolution NMR spectroscopy of encapsulated proteins and nucleic acids dissolved in low-viscosity fluids.
Optimized reverse micelle surfactant system for high-resolution NMR spectroscopy of encapsulated proteins and nucleic acids dissolved in low-viscosity fluids.
Related ArticlesOptimized reverse micelle surfactant system for high-resolution NMR spectroscopy of encapsulated proteins and nucleic acids dissolved in low-viscosity fluids.
J Am Chem Soc. 2014 Feb 4;
Authors: Dodevski I, Nucci NV, Valentine KG, Sidhu GK, O'Brien ES, Pardi A, Wand AJ
Abstract
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. Comprised of 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 ultra-low viscosity liquid ethane and therefore will serve as a general surfactant system for initiating solution NMR studies of proteins and nucleic acids.
PMID: 24495164 [PubMed - as supplied by publisher]
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids
Abstract Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30 kDa require complex experimental methods, such as TROSY in conjunction with isotopic labeling schemes that are often expensive and generally reduce the potential information available. We have developed the reverse micelle encapsulation strategy as an alternative approach. Encapsulation of...
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07-15-2011 09:10 PM
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
J Biomol NMR. 2011 Jul 12;
Authors: Nucci NV, Marques BS, Bédard S, Dogan J, Gledhill JM, Moorman VR, Peterson RW, Valentine KG, Wand AL, Wand AJ
Comprehensive application of solution NMR spectroscopy to studies of macromolecules remains fundamentally limited by the molecular rotational correlation time. For proteins, molecules larger than 30*kDa require complex...
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07-13-2011 06:42 PM
[NMR paper] Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
Related Articles Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
Protein Sci. 2005 Nov;14(11):2919-21
Authors: Peterson RW, Pometun MS, Shi Z, Wand AJ
NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids is emerging as a tool for biophysical studies of proteins in atomic detail in a variety of otherwise inaccessible contexts. The central element of the...
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12-01-2010 06:56 PM
[NMR paper] High-resolution NMR studies of encapsulated proteins in liquid ethane.
High-resolution NMR studies of encapsulated proteins in liquid ethane.
High-resolution NMR studies of encapsulated proteins in liquid ethane.
J Am Chem Soc. 2005 Jul 27;127(29):10176-7
Authors: Peterson RW, Lefebvre BG, Wand AJ
Many of the difficulties presented by large, aggregation-prone, and membrane proteins to modern solution NMR spectroscopy can be alleviated by actively seeking to increase the effective rate of molecular reorientation. An emerging approach involves encapsulating the protein of interest within the protective shell of a...
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[NMR paper] NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
Related Articles NMR spectroscopy of proteins encapsulated in a positively charged surfactant.
J Magn Reson. 2005 Jul;175(1):158-62
Authors: Lefebvre BG, Liu W, Peterson RW, Valentine KG, Wand AJ
Traditionally, large proteins, aggregation-prone proteins, and membrane proteins have been difficult to examine by modern multinuclear and multidimensional solution NMR spectroscopy. A major limitation presented by these protein systems is that their slow molecular...
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11-25-2010 08:21 PM
[NMR paper] Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic aci
Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids.
Related Articles Relaxation-optimized NMR spectroscopy of methylene groups in proteins and nucleic acids.
J Am Chem Soc. 2004 Sep 1;126(34):10560-70
Authors: Miclet E, Williams Jr DC, Clore GM, Bryce DL, Boisbouvier J, Bax A
A large fraction of hydrogens in proteins and nucleic acids is of the methylene type. Their detailed study, however, in terms of structure and dynamics by NMR spectroscopy is hampered by their fast relaxation properties, which give...
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11-24-2010 10:01 PM
[NMR paper] A simple and effective NMR cell for studies of encapsulated proteins dissolved in low
A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents.
Related Articles A simple and effective NMR cell for studies of encapsulated proteins dissolved in low viscosity solvents.
J Biomol NMR. 2002 Aug;23(4):311-6
Authors: Flynn PF, Milton MJ, Babu CR, Wand AJ
Application of triple-resonance and isotope-edited-NOE methods to the study of increasingly larger macromolecules and their complexes remains a central goal of solution NMR spectroscopy. The slow reorientational motion of larger molecules...
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11-24-2010 08:58 PM
[NMR paper] High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
Related Articles High-resolution NMR of encapsulated proteins dissolved in low-viscosity fluids.
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15299-302
Authors: Wand AJ, Ehrhardt MR, Flynn PF
The majority of known proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution. Here we introduce an approach to making the NMR relaxation properties of large proteins amenable to modern solution NMR...
Optimized reverse micelle surfactant system for high-resolution NMR spectroscopy of encapsulated proteins and nucleic acids dissolved in low-viscosity fluids.
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