OptimizedReverse Micelle Surfactant System for High-ResolutionNMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolvedin Low Viscosity Fluids
OptimizedReverse Micelle Surfactant System for High-ResolutionNMR Spectroscopy of Encapsulated Proteins and Nucleic Acids Dissolvedin Low Viscosity Fluids
[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 Articles Optimized 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...
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02-06-2014 12:47 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
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] 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] 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...