Related ArticlesNovel 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 approach is the encapsulation of the protein of interest within the aqueous core of a reverse micelle with high structural fidelity. The process of encapsulation is highly dependent upon the nature of the surfactant(s) employed. Here we describe novel mixtures of surfactants that are capable of successfully encapsulating a range of types of proteins under a variety of conditions.
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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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] 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] Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolve
Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
Related Articles Preparation, characterization, and NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.
J Biomol NMR. 2003 Apr;25(4):313-23
Authors: Babu CR, Flynn PF, Wand AJ
Encapsulating a protein in a reverse micelle and dissolving it in a low-viscosity solvent can lower the rotational correlation time of a protein and thereby provides a novel strategy for studying proteins in a variety of contexts. The...
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11-24-2010 09:01 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...
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11-17-2010 11:15 PM
[NMR paper] What NMR can tell us about where lung surfactant proteins live.
What NMR can tell us about where lung surfactant proteins live.
Related Articles What NMR can tell us about where lung surfactant proteins live.
Biochem Soc Trans. 1997 Aug;25(3):1103-7
Authors: Morrow MR, Taneva S, Dico AS, Hancock J, Keough KM
2H-NMR is beginning to provide some insights into the way in which the hydrophobic surfactant proteins SP-B and SP-C interact with phospholipid bilayers in multilamellar structures. Both proteins have a significant effect on slow bilayer motions. In many ways, the effect of SP-C on the surrounding...
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08-22-2010 05:08 PM
[NMR paper] Analysis of biological fluids using 600 MHz proton NMR spectroscopy: application of h
Analysis of biological fluids using 600 MHz proton NMR spectroscopy: application of homonuclear two-dimensional J-resolved spectroscopy to urine and blood plasma for spectral simplification and assignment.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Analysis of biological fluids using 600 MHz proton NMR spectroscopy: application of homonuclear two-dimensional J-resolved spectroscopy to urine and blood plasma for spectral simplification and assignment.
J Pharm Biomed Anal. 1993...
Novel surfactant mixtures for NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.
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