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Detergents schematic representation

Fig. 3.1. Schematic representation of normal micelle (M) in water, a soft-core reverse micelle (RM) and hard-core reverse micelles (RM) in hydrocarbon formulation, ( AAAO ) detergent molecule... Fig. 3.1. Schematic representation of normal micelle (M) in water, a soft-core reverse micelle (RM) and hard-core reverse micelles (RM) in hydrocarbon formulation, ( AAAO ) detergent molecule...
Fig. 2 Schematic representation of potential changes in integral membrane protein structure that could be imposed by a micellar environment (left hand side of each panel), compared to the native structure in bilayers (right). Possible distortions include (a) micelle-induced curvature in the TM helix or amphipathic helix (b) monomeric detergent molecules bound to a solvent-exposed region, in this case an aqueous cavity close to the micelle surface (c) altered relative orientations of amphipathic vs TM helices (d) loss of tilt relative to other TM segments. In this scenario hydrophobic mismatch between the TM helix and micelle are minimized by distortions in micelle structure that allow hydrophobic protein surfaces to remain in the hydrophobic phase. In the bilayer environment hydrophobic mismatch induces tilt, favoring a non-zero inter-helical crossing angles... Fig. 2 Schematic representation of potential changes in integral membrane protein structure that could be imposed by a micellar environment (left hand side of each panel), compared to the native structure in bilayers (right). Possible distortions include (a) micelle-induced curvature in the TM helix or amphipathic helix (b) monomeric detergent molecules bound to a solvent-exposed region, in this case an aqueous cavity close to the micelle surface (c) altered relative orientations of amphipathic vs TM helices (d) loss of tilt relative to other TM segments. In this scenario hydrophobic mismatch between the TM helix and micelle are minimized by distortions in micelle structure that allow hydrophobic protein surfaces to remain in the hydrophobic phase. In the bilayer environment hydrophobic mismatch induces tilt, favoring a non-zero inter-helical crossing angles...
FIGURE 20.3 Schematic representation of the differential detergent fractionation procedure applied to cultured cells. Four fractions are obtained (1) cytosolic proteins, (2) membrane/organelle proteins, (3) nuclear-membrane proteins, and (4) cytoskeletal proteins. (Modified from Fazal, M. A., et al., J. Chwmatogr. A, 1130, 182-189,2006.)... [Pg.588]

For this purpose we first examine the effect of micellar dissolution of alcohols on micelle stability. This can be conveniently done by means of the schematic representation of part of an alcohol + detergent mixed micelle shown in Figure 7. It has been assumed that alcohol molecules dissolved into micelles have their hydroxyl group at the micelle surface or in the palissade layer (this may not be always the case, as is discussed below). The first effect of the dissolved alcohol molecules is a steric effect. Indeed alcohol molecules intercalated between ionic head groups may push them farther apart than in the absence of alcohol. This would result in a decrease of the surface charge density and a release of counterions, that is an increase of a. This steric effect may not be too important as long as not too many alcohol molecules are... [Pg.527]

Figure 5.3.14 Schematic representation of the function of detergent molecules (a) basic structure of a detergent molecule (b) oil-in-water micelle ... Figure 5.3.14 Schematic representation of the function of detergent molecules (a) basic structure of a detergent molecule (b) oil-in-water micelle ...
Figure 6.16 Schematic representation of the possible orientation of a tyrothricin molecule at the micellar interface between the hydrophobic core and the hydrophilic envelope of a non-ionic detergent. After Ullmann et al [107]. Figure 6.16 Schematic representation of the possible orientation of a tyrothricin molecule at the micellar interface between the hydrophobic core and the hydrophilic envelope of a non-ionic detergent. After Ullmann et al [107].
Fig. 2 Schematic representation of most common membrane-mimicking environments cmnpatible with solution and/or solid-state NMR studies of integral membrane proteins. Micelle (a), bicelle (b), nanolipoprotein particles also known as nanodiscs (c), and liposomes (d). The membrane protein is depicted in gray, detergents are colored in brown and lipids in blue. The apolipoprotein also known as membrane scaffold protein is represented as a green ring. Liposomes are scaled down by a factor of 2... Fig. 2 Schematic representation of most common membrane-mimicking environments cmnpatible with solution and/or solid-state NMR studies of integral membrane proteins. Micelle (a), bicelle (b), nanolipoprotein particles also known as nanodiscs (c), and liposomes (d). The membrane protein is depicted in gray, detergents are colored in brown and lipids in blue. The apolipoprotein also known as membrane scaffold protein is represented as a green ring. Liposomes are scaled down by a factor of 2...

See other pages where Detergents schematic representation is mentioned: [Pg.521]    [Pg.277]    [Pg.243]    [Pg.437]    [Pg.588]    [Pg.529]    [Pg.318]    [Pg.724]    [Pg.293]    [Pg.25]   
See also in sourсe #XX -- [ Pg.500 ]




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Schematic representation

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