[NMR paper] Structure of pravastatin and its complex with sodium dodecyl sulfate micelles studied by NMR spectroscopy.
Structure of pravastatin and its complex with sodium dodecyl sulfate micelles studied by NMR spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary_FullTextOnline_120x27.gif Related Articles Structure of pravastatin and its complex with sodium dodecyl sulfate micelles studied by NMR spectroscopy.
Magn Reson Chem. 2015 Feb;53(2):110-4
Authors: Galiullina LF, Rakhmatullin IZ, Klochkova EA, Aganov AV, Klochkov VV
Abstract
The aim of this work was...
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09-30-2015 10:34 PM
[NMR paper] Synthesis of uniformly deuterated n-dodecyl-?-D-maltoside (d39 -DDM) for solubilization of membrane proteins in TROSY NMR experiments.
Synthesis of uniformly deuterated n-dodecyl-?-D-maltoside (d39 -DDM) for solubilization of membrane proteins in TROSY NMR experiments.
Related Articles Synthesis of uniformly deuterated n-dodecyl-?-D-maltoside (d39 -DDM) for solubilization of membrane proteins in TROSY NMR experiments.
J Labelled Comp Radiopharm. 2014 Dec 9;
Authors: Hiruma-Shimizu K, Kalverda AP, Henderson PJ, Homans SW, Patching SG
Abstract
This work reports the first synthesis of uniformly deuterated n-dodecyl-?-D-maltoside (d39 -DDM). DDM is a mild non-ionic...
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12-11-2014 11:22 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
[NMR paper] Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs.
Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs.
Biochim Biophys Acta. 2012 Jun;1818(6):1562-9
Authors: Yu TY, Raschle T, Hiller S, Wagner G
Abstract
Three isoforms of the human voltage-dependent anion channel (VDAC), located...
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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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[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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11-24-2010 09:16 PM
[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...
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11-17-2010 11:06 PM
[NMR paper] Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Related Articles Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.
Biochemistry. 1994 Nov 8;33(44):12990-7
Authors: Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ
The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS...
Dodecyl-?-melibioside Detergent Micelles asa Medium for Membrane Proteins
Linear Mode
