Peripheral membrane proteins (PMPs) are a subgroup of membrane-associated proteins that are water-soluble and bind to membranes, often reversibly, to perform their function. These proteins have been extensively studied in the aqueous state, but there is often a lack of high-resolution structural and functional studies of these proteins in the membrane-bound state. Currently, nuclear magnetic resonance (NMR) is among the best-equipped methods to study these relatively small proteins and domains,...
[NMR paper] A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains.
A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains.
Related Articles A generalized approach for NMR studies of lipid-protein interactions based on sparse fluorination of acyl chains.
Chem Commun (Camb). 2018 Jun 15;:
Authors: De Biasio A, Ibáńez de Opakua A, Bostock MJ, Nietlispach D, Diercks T, Blanco FJ
Abstract
Sparse lipid fluorination enhances the lipids' 1H signal dispersion, enables clean molecular distinction by 19F NMR, and evinces micelle insertion of...
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06-16-2018 08:02 PM
[NMR paper] Interrogating membrane protein conformational dynamics within native lipid compositions
Interrogating membrane protein conformational dynamics within native lipid compositions
Membrane protein-lipid interplay is important for cellular function, however, tools enabling the interrogation of protein dynamics within native lipid environments are scarce and often invasive. We establish that the styrene-maleic acid anhydride lipid particle (SMALP) technology can be coupled with hydrogen-deuterium exchange mass spectrometry (HDX-MS) to investigate membrane protein conformational dynamics within native lipid bilayers. We demonstrate changes in accessibility and dynamics of the...
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10-19-2017 10:47 PM
[NMR paper] Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Related Articles Solution-NMR Characterization of Outer-Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles.
Chembiochem. 2014 Apr 1;
Authors: Sušac L, Horst R, Wüthrich K
Abstract
X-ray crystallography and solution NMR of detergent-reconstituted OmpA (outer membrane protein A from E. coli) had shown that this protein forms an eight-stranded transmembrane ?-barrel, but only...
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04-03-2014 12:59 PM
Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins
From The DNP-NMR Blog:
Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins
Valentine, K.G., et al., Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins. J Am Chem Soc, 2014. 136(7): p. 2800-7.
http://pubs.acs.org/doi/abs/10.1021/ja4107176
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03-27-2014 03:46 AM
[NMR paper] Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
Related Articles Reverse micelles as a platform for dynamic nuclear polarization in solution NMR of proteins.
J Am Chem Soc. 2014 Jan 24;
Authors: Valentine KG, Mathies G, Bédard S, Nucci NV, Dodevski I, Stetz MA, Can TV, Griffin RG, Wand AJ
Abstract
Despite tremendous advances in recent years, solution NMR remains fundamentally restricted due to its inherent insensitivity. Dynamic nuclear polarization (DNP) potentially offers significant...
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01-25-2014 02:07 PM
Modification of Encapsulation Pressure of Reverse Micelles in Liquid Ethane
Modification of Encapsulation Pressure of Reverse Micelles in Liquid Ethane
Publication year: 2011
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 20 June 2011</br>
Ronald W., Peterson , Nathaniel V., Nucci , A., Joshua Wand</br>
A central motivation for employing samples of encapsulated proteins dissolved in low viscosity fluids for high resolution NMR spectroscopy is to benefit from the superior performance afforded by the faster macromolecular rotation of the encapsulated protein than it has in free aqueous solution. Encapsulation of...
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06-22-2011 03:40 AM
[NMR paper] Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy wit
Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.
Related Articles Membrane protein-lipid interactions in mixed micelles studied by NMR spectroscopy with the use of paramagnetic reagents.
Chembiochem. 2004 Apr 2;5(4):467-73
Authors: Hilty C, Wider G, Fernández C, Wüthrich K
For solution NMR studies of the structure and function of membrane proteins, these macromolecules have to be reconstituted and solubilized in detergent micelles. Detailed characterization of the mixed...
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11-24-2010 09:51 PM
[NMR paper] Lipid-protein interactions in DHPC micelles containing the integral membrane protein
Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.
Related Articles Lipid-protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13533-7
Authors: Fernández C, Hilty C, Wider G, Wüthrich K
Intermolecular nuclear Overhauser effects (NOEs) between the integral outer membrane protein OmpX from Escherichia coli and dihexanoylphosphatidylcholine (DHPC) provided a detailed...
An NMR Approach for Investigating Membrane Protein-Lipid Interactions Using Native Reverse Micelles
Linear Mode
