[NMR paper] An NMR Approach for Investigating Membrane Protein-Lipid Interactions Using Native Reverse Micelles
An NMR Approach for Investigating Membrane Protein-Lipid Interactions Using Native Reverse Micelles
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...
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08-05-2024 09:41 PM
Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles
Micro-coil NMR to monitor optimization of the reconstitution conditions for the integral membrane protein OmpW in detergent micelles
Abstract Optimization of aqueous solutions of the integral membrane protein (IMP) OmpW for NMR structure determination has been monitored with micro-coil NMR, which enables the acquisition of NMR spectra using only micrograms of protein and detergent. The detergent 30-Fos (2-undecylphosphocholine) was found to yield the best 2D -TROSY correlation NMR spectra of -labeled OmpW. For the OmpW structure determination we then optimized the 30-Fos concentration,...
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08-16-2012 09:18 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] NMR structure of the integral membrane protein OmpX.
NMR structure of the integral membrane protein OmpX.
Related Articles NMR structure of the integral membrane protein OmpX.
J Mol Biol. 2004 Mar 5;336(5):1211-21
Authors: Fernández C, Hilty C, Wider G, Güntert P, Wüthrich K
The structure of the integral membrane protein OmpX from Escherichia coli reconstituted in 60 kDa DHPC micelles (OmpX/DHPC) was calculated from 526 NOE upper limit distance constraints. The structure determination was based on complete sequence-specific assignments for the amide protons and the Val, Leu, and Ile(delta1)...
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11-24-2010 09:25 PM
[NMR paper] Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelle
Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
Related Articles Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles.
J Biomol NMR. 2002 Aug;23(4):289-301
Authors: Hilty C, Fernández C, Wider G, Wüthrich K
Sequence-specific assignments have been obtained for side chain methyl resonances of Val, Leu and Ile in the outer membrane protein X (OmpX) from Escherichia coli reconstituted in 60 kDa micelles in aqueous solution. Using previously established techniques, OmpX was...
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11-24-2010 08:58 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...
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11-24-2010 08:58 PM
[NMR paper] Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia
Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli.
Related Articles Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli.
FEBS Lett. 2001 Aug 31;504(3):173-8
Authors: Fernández C, Hilty C, Bonjour S, Adeishvili K, Pervushin K, Wüthrich K
Membrane proteins are usually solubilized in polar solvents by incorporation into micelles. Even for small membrane proteins these mixed micelles have rather large molecular masses, typically beyond 50000 Da. The NMR technique TROSY...
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11-19-2010 08:44 PM
[NMR paper] Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX
Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles.
Related Articles Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles.
Proc Natl Acad Sci U S A. 2001 Feb 27;98(5):2358-63
Authors: Fernández C, Adeishvili K, Wüthrich K
The (2)H,(13)C,(15)N-labeled, 148-residue integral membrane protein OmpX from Escherichia coli was reconstituted with dihexanoyl phosphatidylcholine (DHPC) in mixed micelles...
Lipid–protein interactions in DHPC micelles containing the integral membrane protein OmpX investigated by NMR spectroscopy - pnas.org
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