Related ArticlesOn 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 spanned a fairly limited range of values: 2.7 to 4.7 (x10(-7) cm2/s). No general correlation was observed between the diffusion coefficients for the detergent-DAGK aggregates and the sizes of the corresponding protein-free micelles. These results indicate that the effective molecular weights of the DAGK-detergent aggregates were determined more by the structural properties of the protein than by the properties of the detergents. The catalytic activity of DAGK in detergents having medium-length alkyl chains such as dodecylphosphocholine or decylmaltoside was usually observed to be substantially higher than in short-chain detergents such as octylphosphocholine or octylglucoside. Taken together, the diffusion and activity results indicate that medium-chain detergents are generally preferred for use in NMR studies of complex membrane proteins because they are no worse than short-chained detergents in terms of increasing the effective molecular weight of the protein of interest while they are considerably better at maintaining native-like protein conformation. Among the 10 detergents examined, only sodium dodecylsulfate was observed to be unable to support DAGK activity under any conditions examined, suggest that this well-known protein denaturant should be used with care in studies of complex membrane proteins.
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...
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
04-12-2011 11:08 AM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins.
J Am Chem Soc. 2011 Feb 2;
Authors: Shi L, Traaseth NJ, Verardi R, Gustavsson M, Gao J, Veglia G
Residual dipolar couplings (RDCs) are widely used as orientation-dependent NMR restraints to improve the resolution of the NMR conformational ensemble of biomacromolecules and define the...
nmrlearner
Journal club
0
02-04-2011 11:34 AM
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Paramagnetic-Based NMR Restraints Lift Residual Dipolar Coupling Degeneracy in Multidomain Detergent-Solubilized Membrane Proteins
Lei Shi, Nathaniel J. Traaseth, Raffaello Verardi, Martin Gustavsson, Jiali Gao and Gianluigi Veglia
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109080t/aop/images/medium/ja-2010-09080t_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109080t
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/Tu9H79dfKCk
nmrlearner
Journal club
0
02-03-2011 06:45 AM
[NMR paper] NMR study of a membrane protein in detergent-free aqueous solution.
NMR study of a membrane protein in detergent-free aqueous solution.
Related Articles NMR study of a membrane protein in detergent-free aqueous solution.
Proc Natl Acad Sci U S A. 2005 Jun 21;102(25):8893-8
Authors: Zoonens M, Catoire LJ, Giusti F, Popot JL
One of the major obstacles to membrane protein (MP) structural studies is the destabilizing effect of detergents. Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep MPs water-soluble under mild conditions. In the present work, we have explored the...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[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...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] Detergent-resistant membrane fractions contribute to the total 1H NMR-visible lipid s
Detergent-resistant membrane fractions contribute to the total 1H NMR-visible lipid signal in cells.
Related Articles Detergent-resistant membrane fractions contribute to the total 1H NMR-visible lipid signal in cells.
Eur J Biochem. 2003 May;270(9):2091-100
Authors: Wright LC, Djordjevic JT, Schibeci SD, Himmelreich U, Muljadi N, Williamson P, Lynch GW
Leukocytes and other cells show an enhanced intensity of mobile lipid in their 1H NMR spectra under a variety of conditions. Such conditions include stimulation, which has recently been shown...
nmrlearner
Journal club
0
11-24-2010 09:01 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...