Related ArticlesAn evaluation of detergents for NMR structural studies of membrane proteins.
J Biomol NMR. 2004 Jan;28(1):43-57
Authors: Krueger-Koplin RD, Sorgen PL, Krueger-Koplin ST, Rivera-Torres IO, Cahill SM, Hicks DB, Grinius L, Krulwich TA, Girvin ME
Structural information on membrane proteins lags far behind that on soluble proteins, in large part due to difficulties producing homogeneous, stable, structurally relevant samples in a membrane-like environment. In this study 25 membrane mimetics were screened using 2D (1)H-(15)N heteronuclear single quantum correlation NMR experiments to establish sample homogeneity and predict fitness for structure determination. A single detergent, 1-palmitoyl-2-hydroxy-sn-glycero-3-[phospho-RAC-(1-glycerol)] (LPPG), yielded high quality NMR spectra with sample lifetimes greater than one month for the five proteins tested - R. sphaeroides LH1 alpha and beta subunits, E. coli and B. pseudofirmus OF4 ATP synthase c subunits, and S. aureus small multidrug resistance transporter - with 1, 2, or 4 membrane spanning alpha-helices, respectively. Site-specific spin labeling established interhelical distances in the drug transporter and genetically fused dimers of c subunits in LPPG consistent with in vivo distances. Optical spectroscopy showed that LH1 beta subunits form native-like complexes with bacteriochlorophyll a in LPPG. All the protein/micelle complexes were estimated to exceed 100 kDaltons by translational diffusion measurements. However, analysis of (15)N transverse, longitudinal and (15)N[(1)H] nuclear Overhauser effect relaxation measurements yielded overall rotational correlation times of 8 to 12 nsec, similar to a 15-20 kDalton protein tumbling isotropically in solution, and consistent with the high quality NMR data observed.
Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Curr Opin Struct Biol. 2011 Jul 18;
Authors: Nietlispach D, Gautier A
NMR spectroscopy has established itself as one of the main techniques for the structural study of integral membrane proteins. Remarkably, over the last few years, substantial progress has been achieved in the structure determination of increasingly complex polytopical ?-helical membrane proteins, with their size approaching ~100kDa. Such advances are the...
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07-23-2011 08:54 AM
Choosing membrane mimetics for NMR structural studies of transmembrane proteins.
Choosing membrane mimetics for NMR structural studies of transmembrane proteins.
Choosing membrane mimetics for NMR structural studies of transmembrane proteins.
Biochim Biophys Acta. 2011 Apr 5;
Authors: Warschawski DE, Arnold AA, Beaugrand M, Gravel A, Chartrand E, Marcotte I
The native environment of membrane proteins is complex and scientists have felt the need to simplify it to reduce the number of varying parameters. However, experimental problems can also arise from oversimplification which contributes to why membrane proteins are...
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04-12-2011 11:08 AM
[NMR paper] Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
Related Articles Solid-state 17O NMR as a probe for structural studies of proteins in biomembranes.
J Am Chem Soc. 2004 Dec 1;126(47):15320-1
Authors: Lemaître V, de Planque MR, Howes AP, Smith ME, Dupree R, Watts A
We report the first example of 17O NMR spectra from a selectively labeled transmembrane peptide, 17O--WALP23, as a lyophilized powder and incorporated in hydrated phospholipid vesicles. It is shown that at high magnetic field it is feasible to apply...
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11-24-2010 10:03 PM
[NMR paper] Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals to
Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with amino acid residues.
Related Articles Site-directed 13C solid-state NMR studies on membrane proteins: strategy and goals toward revealing conformation and dynamics as illustrated for bacteriorhodopsin labeled with amino acid residues.
Magn Reson Chem. 2004 Feb;42(2):218-30
Authors: Saitô H, Mikami J, Yamaguchi S, Tanio M, Kira A, Arakawa T, Yamamoto K, Tuzi S
We have so...
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11-24-2010 09:25 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] NMR structural studies on antifreeze proteins.
NMR structural studies on antifreeze proteins.
Related Articles NMR structural studies on antifreeze proteins.
Biochem Cell Biol. 1998;76(2-3):284-93
Authors: Sönnichsen FD, Davies PL, Sykes BD
Antifreeze proteins (AFPs) are a structurally diverse class of proteins that bind to ice and inhibit its growth in a noncolligative manner. This adsorption-inhibition mechanism operating at the ice surface results in a lowering of the (nonequilibrium) freezing point below the melting point. A lowering of approximately 1 degree C, which is sufficient to...
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11-17-2010 11:06 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...
An evaluation of detergents for NMR structural studies of membrane proteins.
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