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Pink model

The Pink model is found to exhibit a gel-fluid transition for lipids with sufficiently long chains, which is weakly first order. The transition disappears in bilayers of shorter lipids, but it leaves a signature in that one observes strong lateral density fluctuations in a narrow temperature region [200,201]. In later studies, the model has been extended in many ways in order to explore various aspects of gel-fluid transitions [202]. For example, Mouritsen et al. [203] have investigated the interplay between chain melting and chain crystallization by coupling a two-state Doniach model or a ten-state Pink model to a Potts model. (The use of Potts models as models for... [Pg.664]

Fig. 17.7 The calculated solubility of C02 in water at 1 atm using the Steele [24] C02 [down triangle, green] model with TIP3P water, the developed C02(TIP3P) [up triangle, blue], C02(TIP4P) [circle, red], C02(TIP4P-Ew)[left pointing triangle, pink] models with their respective water models, compared against the experimental values [square, black] [25, 26]... Fig. 17.7 The calculated solubility of C02 in water at 1 atm using the Steele [24] C02 [down triangle, green] model with TIP3P water, the developed C02(TIP3P) [up triangle, blue], C02(TIP4P) [circle, red], C02(TIP4P-Ew)[left pointing triangle, pink] models with their respective water models, compared against the experimental values [square, black] [25, 26]...
At the bar at Pop Burger, a model-svelte, South Beach North—style burger joint in the meatpacking distinct, I ordered four house specials the Pink Panty Pulldown, the Cosmopolitang, the Flirtini and the Union Cocktail—I m assuming as in suit. Pop Burger, which has a take-out counter up front, has a lounge in the back—McDonald s with a velvet rope. [Pg.98]

For quantitative work, it is necessary to estimate the concentration of 5-amino-l-(P-D-ribofuranosyl)imidazole in aqueous solution. It seems that the only available method is the Bratton-Marshall assay, which was originally developed for the estimation of arylamines in biological fluids. The principle of the method is the spectrometric estimation of a salmon-pink colored dyestuff obtained by diazotation in situ, followed by coupling with /V-( 1 -naphthyl)ethyl-enediamine.65 The only remaining problem then is to know the molar extinction of this dye because pure samples of AIRs are not available. A value of 16800 at 520 nM was obtained for the dyes prepared from a model compound, 5-amino-l-cyclohexylimidazole-4-carboxylic acid (54), which is crystalline. A comparable molar extinction can be expected for the dye prepared from imidazole 55, if the carboxyl group does not exert too much influence on the chromophore. Actually, its influence is perceptible even with the naked eye, the dyestuff prepared from 53 having a somewhat different, wine-red color, with max>520 nM. The molar extinction for 55 is 17400 at 500 nM. When the decarboxylation of 54 was conducted under mild acidic conditions (pH 4.8, 50°C, 1 hour), estimation of 5-aminoimidazole 55 by the Bratton-Marshall method led to the conclusion that the reaction was almost quantitative.66 Similar conditions for the final decarboxylation were adopted in the preparation of samples of AIRs labeled with stable isotopes.58... [Pg.299]

Brilliant, M. H. (1992). The mouse pink-eyed dilution locus—a model for aspects of Prader-Willi-syndrome, Angelman syndrome, and a form of hypomelanosis of Ito. Mamm. Genome 3 187-191. [Pg.172]

Figure 6.8 Stereoscopic view of the dimeric building block of bacterioferritin (a) twofold axis horizontal (b) twofold axis approximately normal to the page. The protein is represented by a blue a-carbon trace, the haem by a stick model (pink) and the dinuclear metal site by dotted spheres (orange and yellow). From Frolow et ah, 1994. Reproduced by permission of Nature Publishing Group. Figure 6.8 Stereoscopic view of the dimeric building block of bacterioferritin (a) twofold axis horizontal (b) twofold axis approximately normal to the page. The protein is represented by a blue a-carbon trace, the haem by a stick model (pink) and the dinuclear metal site by dotted spheres (orange and yellow). From Frolow et ah, 1994. Reproduced by permission of Nature Publishing Group.
The new work has established that a neurodegenerative pathway leading from soluble to insoluble, filamentous a-synuclein is central to Lewy body diseases and multiple system atrophy. The development of experimental models of a-synucleinopathies has opened the way to the identification of the detailed mechanisms by which the formation of inclusions causes disease. These model systems have also made it possible to identify disease modifiers that may well lead to the development of the first mechanism-based therapies for these diseases. At a conceptual level, it will be important to understand whether a-synuclein has a role to play in disorders, such as autosomal-recessive juvenile forms of parkinsonism caused by mutations in the Parkin, DJ-1 and PINK-1 genes, or whether there are entirely separate mechanisms by which the dopaminergic nerve cells of the substantia nigra degenerate in Parkinson s disease and in inherited disorders with parkinsonism. [Pg.751]

Pink JJ, Jordan VC (1996) Models of estrogen receptor regulation by estrogens and antiestrogens in breast cancer cell fines. Cancer Res 56 2321-2330... [Pg.167]

Abstract Why do patients refer to medications as the little white pill or the pink capsule Strange or confusing names are problematic especially if you are old and have many medications. Other potential practical medication problems in the elderly including problems to remember, to swallow, practical handling, food- and drug-interactions, short use-before date are listed and described in this chapter. Possible solutions are also presented. For patient safety and for cost-effective care it s very important to identify and solve these problems for the individual patient. A systematic model for this is presented in Chapter 10. [Pg.101]

Two of these systems were studied as models—the acetylation of choline in brain to give acetyl choline (Hebb, Nachmansohn), and of sulfanilamide (the active component in prontosil, Chapter 3) in liver (Lipmann). Sulfanilamide is rapidly inactivated by acetylation on the p-amino group and then excreted. Sulfanilamide is easily diazotized the diazonium salt formed can be coupled with N-( 1 -naphthyl)ethylenedi-amine dihydrochloride to give a pink derivative (Bratton and Marshall, 1939). This formed the basis for an elegant colorimetric assay. Only the free p-amino group reacts, so that as acetylation proceeded color formation diminished. [Pg.78]

The van der Waals model of monomeric insulin (1) once again shows the wedge-shaped tertiary structure formed by the two chains together. In the second model (3, bottom), the side chains of polar amino acids are shown in blue, while apolar residues are yellow or pink. This model emphasizes the importance of the hydrophobic effect for protein folding (see p. 74). In insulin as well, most hydrophobic side chains are located on the inside of the molecule, while the hydrophilic residues are located on the surface. Apparently in contradiction to this rule, several apolar side chains (pink) are found on the surface. However, all of these residues are involved in hydrophobic interactions that stabilize the dimeric and hexameric forms of insulin. [Pg.76]

We must now define the model for the diode. Click the LEFT mouse button on the diode graphic, —W—. The graphic should turn pink, indicating that it has been selected. Next, select Edit and then PSpice Model from the Capture menus ... [Pg.175]

Now that we have copied the text, we can paste it into a model in Capture. Switch back to Capture and select the Dbreak part. It should be highlighted in pink when selected ... [Pg.452]

Fig. 1. We show on the left-hand side the MLWCs (above) in pink and the HOMO-Wannier orbital (below) together with a ball-and-stick model of a I-DMSO-3-H2O water cluster. On the right the same is depicted for the [PdCl2(NH3)]2 complex. Fig. 1. We show on the left-hand side the MLWCs (above) in pink and the HOMO-Wannier orbital (below) together with a ball-and-stick model of a I-DMSO-3-H2O water cluster. On the right the same is depicted for the [PdCl2(NH3)]2 complex.
Figure 15.9. Superimposition of 3D protein structures at CE server. The opening graphic window for the superimposition of the modeled (homology modeling with SPDBV) pigeon lysozyme (USR2 in pink) and hen s egg-white lysozyme, ILYZ.pdb (USR1 in blue). The superimposed structures are displayed with the alignment summary (e.g., sequence identity, rms deviation). Figure 15.9. Superimposition of 3D protein structures at CE server. The opening graphic window for the superimposition of the modeled (homology modeling with SPDBV) pigeon lysozyme (USR2 in pink) and hen s egg-white lysozyme, ILYZ.pdb (USR1 in blue). The superimposed structures are displayed with the alignment summary (e.g., sequence identity, rms deviation).
Fig. 7 The location on tubulin of residues that modulate the sensitivity to MT-destabilizing agents and the location of exogenous inhibitor and nucleotide sites on P tubulin. The a subunit is in semitransparent pink together with a composite P-subunit color-coded as in Fig. 3a with ball-and-stick models of bound taxol (orange), colchicine (yellow) and GDP (magenta). Ball-and-stick models of vinblastine (cyan) are drawn on the two partial vinca sites on a and on P tubulin. The sulfur atom of Cys P12 is highlighted as a yellow sphere. The sites of nine amino acid substitutions [49] that both confer resistance to vinblastine and colchicine and stabilize MTs are depicted as red (on a tubulin) or green (on P tubulin) spheres. Two residues of the P H10 helix whose mutations enhance the sensitivity to colchicine site ligands and destabilize MTs [71] are also shown as blue spheres... Fig. 7 The location on tubulin of residues that modulate the sensitivity to MT-destabilizing agents and the location of exogenous inhibitor and nucleotide sites on P tubulin. The a subunit is in semitransparent pink together with a composite P-subunit color-coded as in Fig. 3a with ball-and-stick models of bound taxol (orange), colchicine (yellow) and GDP (magenta). Ball-and-stick models of vinblastine (cyan) are drawn on the two partial vinca sites on a and on P tubulin. The sulfur atom of Cys P12 is highlighted as a yellow sphere. The sites of nine amino acid substitutions [49] that both confer resistance to vinblastine and colchicine and stabilize MTs are depicted as red (on a tubulin) or green (on P tubulin) spheres. Two residues of the P H10 helix whose mutations enhance the sensitivity to colchicine site ligands and destabilize MTs [71] are also shown as blue spheres...

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See also in sourсe #XX -- [ Pg.664 ]




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