Related ArticlesThe Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media.
J Membr Biol. 2014 Mar 28;
Authors: Planchard N, Point E, Dahmane T, Giusti F, Renault M, Le Bon C, Durand G, Milon A, Guittet E, Zoonens M, Popot JL, Catoire LJ
Abstract
Solution-state nuclear magnetic resonance studies of membrane proteins are facilitated by the increased stability that trapping with amphipols confers to most of them as compared to detergent solutions. They have yielded information on the state of folding of the proteins, their areas of contact with the polymer, their dynamics, water accessibility, and the structure of protein-bound ligands. They benefit from the diversification of amphipol chemical structures and the availability of deuterated amphipols. The advantages and constraints of working with amphipols are discussed and compared to those associated with other non-conventional environments, such as bicelles and nanodiscs.
PMID: 24676477 [PubMed - as supplied by publisher]
[NMR paper] Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Structure determination of ?-helical membrane proteins by solution-state NMR: Emphasis on retinal proteins.
Biochim Biophys Acta. 2013 Jul 2;
Authors: Gautier A
Abstract
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical...
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Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Structure determination of ?–helical membrane proteins by solution-state NMR: Emphasis on retinal proteins
Publication date: Available online 2 July 2013
Source:Biochimica et Biophysica Acta (BBA) - Bioenergetics</br>
Author(s): Antoine Gautier</br>
The biochemical processes of living cells involve a numerous series of reactions that work with exceptional specificity and efficiency. The tight control of this intricate reaction network stems from the architecture of the proteins that drive the chemical reactions and mediate protein–protein interactions. Indeed, the...
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[NMR paper] Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Solution NMR Studies on the Orientation of Membrane-Bound Peptides and Proteins by Paramagnetic Probes.
Molecules. 2013;18(7):7407-7435
Authors: Schrank E, Wagner GE, Zangger K
Abstract
Many peptides and proteins are attached to or immersed in a biological membrane. In order to understand their function not only the structure but also their topology in the membrane is important. Solution NMR spectroscopy is one of the most often...
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
[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] 15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared
15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins.
Related Articles 15N NMR relaxation studies of calcium-loaded parvalbumin show tight dynamics compared to those of other EF-hand proteins.
Biochemistry. 1998 Jul 14;37(28):9964-75
Authors: Baldellon C, Alattia JR, Strub MP, Pauls T, Berchtold MW, Cavé A, Padilla A
Dynamics of the rat alpha-parvalbumin calcium-loaded form have been determined by measurement of 15N nuclear relaxation using proton-detected heteronuclear NMR...
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[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...
The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media.
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