Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins
Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins
Abstract
Solution NMR spectroscopy has become a robust method to determine structures and explore the dynamics of integral membrane proteins. The vast majority of previous studies on membrane proteins by solution NMR have been conducted in lipid micelles. Contrary to the lipids that form a lipid bilayer in biological membranes, micellar lipids typically contain only a single hydrocarbon chain or two chains that are too short to form a bilayer. Therefore,...
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[NMR paper] Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs.
Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs.
Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs.
Curr Opin Struct Biol. 2013 Aug 7;
Authors: Didenko T, Liu JJ, Horst R, Stevens RC, Wüthrich K
Abstract
Fluorine-19 is a spin-½ NMR isotope with high sensitivity and large chemical shift dispersion, which makes it attractive for high resolution NMR spectroscopy in solution. For studies of membrane proteins it is further of interest that (19)F is rarely found in biological...
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08-13-2013 04:26 PM
Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs
Fluorine-19 NMR of integral membrane proteins illustrated with studies of GPCRs
Publication date: Available online 7 August 2013
Source:Current Opinion in Structural Biology</br>
Author(s): Tatiana Didenko , Jeffrey J Liu , Reto Horst , Raymond C Stevens , Kurt Wüthrich</br>
Fluorine-19 is a spin-½ NMR isotope with high sensitivity and large chemical shift dispersion, which makes it attractive for high resolution NMR spectroscopy in solution. For studies of membrane proteins it is further of interest that 19F is rarely found in biological materials, which...
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08-08-2013 03:41 AM
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] An evaluation of detergents for NMR structural studies of membrane proteins.
An evaluation of detergents for NMR structural studies of membrane proteins.
Related Articles An 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....
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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] On choosing a detergent for solution NMR studies of membrane proteins.
On choosing a detergent for solution NMR studies of membrane proteins.
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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...