Related ArticlesDetergent-resistant membrane fractions contribute to the total 1H NMR-visible lipid signal in cells.
Eur J Biochem. 2003 May;270(9):2091-100
Authors: Wright LC, Djordjevic JT, Schibeci SD, Himmelreich U, Muljadi N, Williamson P, Lynch GW
Leukocytes and other cells show an enhanced intensity of mobile lipid in their 1H NMR spectra under a variety of conditions. Such conditions include stimulation, which has recently been shown to involve detergent-resistant, plasma membrane domains (DRMs) often called lipid rafts. As there is much speculation surrounding the origin of cellular NMR-visible lipid, we analysed subcellular fractions, including DRMs, by NMR spectroscopy. We demonstrated that DRMs isolated by density gradient centrifugation from lymphoid (CEM-T4, stimulated Jurkat cells), and monocytoid (THP-1) cells produced NMR-visible, lipid signals. Large scale subfractionation of THP-1 cells determined that while cytoplasmic lipid droplets constituted much of the total NMR-visible lipid, the contribution of DRMs was significant. Qualitative and quantitative lipid analyses revealed that DRMs and lipid droplets differed in their lipid composition. DRMs were enriched in cholesterol and ganglioside GM1, and contained relatively unsaturated fatty acids compared with the lipid droplets. Both lipid droplets and DRMs contained neutral lipids (triacylgycerols, cholesterol ester, fatty acids in THP-1 cells) that could, in addition to phospholipids, contribute to the NMR-visible lipid. The lipid droplets also exhibited different protein profiles and contained 500-fold less protein than DRMs, confirming that DRMs and droplets were fractionated as separate entities. The NMR-visible lipid in DRMs is therefore unlikely to be a contaminant from lipid droplets. We propose a micropartitioning of the NMR-visible mobile lipid of whole cells between intracellular lipid droplets, where most of this lipid resides, and detergent-resistant plasma membrane domains.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
J Am Chem Soc. 2011 Feb 2;
Authors: Shi L, Traaseth NJ, Verardi R, Gustavsson M, Gao J, Veglia G
Residual dipolar couplings (RDCs) are widely used as orientation-dependent NMR restraints to improve the resolution of the NMR conformational ensemble of biomacromolecules and define the...
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Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Lei Shi, Nathaniel J. Traaseth, Raffaello Verardi, Martin Gustavsson, Jiali Gao and Gianluigi Veglia
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109080t/aop/images/medium/ja-2010-09080t_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109080t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Tu9H79dfKCk
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[NMR paper] NMR study of a membrane protein in detergent-free aqueous solution.
NMR study of a membrane protein in detergent-free aqueous solution.
Related Articles NMR study of a membrane protein in detergent-free aqueous solution.
Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8893-8
Authors: Zoonens M, Catoire LJ, Giusti F, Popot JL
One of the major obstacles to membrane protein (MP) structural studies is the destabilizing effect of detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep MPs water-soluble under mild conditions. In the present work, we have explored the...
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11-25-2010 08:21 PM
[NMR paper] Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cel
Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
Related Articles Proton NMR visible mobile lipid signals in sensitive and multidrug-resistant K562 cells are modulated by rafts.
Cancer Cell Int. 2005 Feb 9;5(1):2
Authors: Mannechez A, Reungpatthanaphong P, de Certaines JD, Leray G, Le Moyec L
BACKGROUND: Most cancer cells are characterized by mobile lipids visible on proton NMR (1H-NMR), these being comprised mainly of methyl and methylene signals from lipid acyl chains....
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11-24-2010 11:14 PM
[NMR paper] 'Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by sol
'Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by solid-state 19F NMR.
Related Articles 'Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by solid-state 19F NMR.
Magn Reson Chem. 2004 Feb;42(2):195-203
Authors: Afonin S, Dürr UH, Glaser RW, Ulrich AS
Solid state (19)F NMR revealed the conformation and alignment of the fusogenic peptide sequence B18 from the sea urchin fertilization protein bindin embedded in flat phospholipid bilayers. Single (19)F labels were introduced into nine...
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[NMR paper] NMR solution structure determination of membrane proteins reconstituted in detergent
NMR solution structure determination of membrane proteins reconstituted in detergent micelles.
Related Articles NMR solution structure determination of membrane proteins reconstituted in detergent micelles.
FEBS Lett. 2003 Nov 27;555(1):144-50
Authors: Fernández C, Wüthrich K
As an alternative to X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy in solution can be used for three-dimensional structure determination of small membrane proteins, preferably proteins with beta-barrel fold. This paper reviews recent achievements as...
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[NMR paper] Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative
Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane.
Related Articles Lipid-protein stoichiometries in a crystalline biological membrane: NMR quantitative analysis of the lipid extract of the purple membrane.
J Lipid Res. 2002 Jan;43(1):132-40
Authors: Corcelli A, Lattanzio VM, Mascolo G, Papadia P, Fanizzi F
The lipid/protein stoichiometries of a naturally crystalline biological membrane, the purple membrane (PM) of Halobacterium salinarum, have been...
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[NMR paper] On choosing a detergent for solution NMR studies of membrane proteins.
On choosing a detergent for solution NMR studies of membrane proteins.
Related Articles On choosing a detergent for solution NMR studies of membrane proteins.
J Biomol NMR. 1998 May;11(4):381-6
Authors: Vinogradova O, Sönnichsen F, Sanders CR
Translational diffusion coefficients and catalytic activities were measured for the integral membrane protein diacylglycerol kinase (DAGK) in a variety of types of detergent micelles. Despite the structural diversity of the detergents examined, the translational diffusion coefficients observed for DAGK...
Detergent-resistant membrane fractions contribute to the total 1H NMR-visible lipid s
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