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Right form

But the key to success Is getting the right form of HBr for the reaction. A lot of people start off with the CA abstract that uses aqueous 70% HBr as the reagent (this abstract is essentially a rewrite of Merck s original patent) [59], The following is the write up ... [Pg.143]

Figure 1.3. The use of quantiles for displaying data. Three distributions of 100 events each are shown in histogram (left) and in quantile (right) form. The reason for choosing the 17 and the 83 - quantiles is explained in the text. Figure 1.3. The use of quantiles for displaying data. Three distributions of 100 events each are shown in histogram (left) and in quantile (right) form. The reason for choosing the 17 and the 83 - quantiles is explained in the text.
Figure 4-3. Oxidative cleavage of adjacent polypeptide chains linked by disulfide bonds (shaded) by per-formic acid (left) or reductive cleavage by 3-mercap-toethanol (right) forms two peptides that contain cysteic acid residues or cysteinyl residues, respectively. Figure 4-3. Oxidative cleavage of adjacent polypeptide chains linked by disulfide bonds (shaded) by per-formic acid (left) or reductive cleavage by 3-mercap-toethanol (right) forms two peptides that contain cysteic acid residues or cysteinyl residues, respectively.
Because Q. [Pg.341]

A 0,(g) is a reactant. The equilibrium system will shift right forming product in an attempt to consume some of the added reactant. Looked at in another way, [02] is increased above its equilibrium value by the addition of oxygen. This makes Qc smaller than Kc. (The [02] is in the denominator of the expression.) And the system shifts right to compensate. [Pg.342]

Endothermic change [AH > 0) An increase in temperature shifts the equilibrium to the right, forming more products. The value of Kc increases. A decrease in temperature shifts the equilibrium to the left, forming more reactants. The value of Kc decreases. [Pg.363]

A decrease in temperature shifts the equilibrium to the right, forming more products. The value of Kc increases. [Pg.363]

Once we have the right form of rate equation, do we have the best values for the rate constants in the equation ... [Pg.75]

Fig. 17.8 Upper Bacterial relics filled with ferri-hydrite, probably from Lepthotrix (left) and Gal-lionella (right), formed by rapid oxidation offerri-ferrous waters of drainage ditches (Susser, Schwertmann, 1983 with permission). Lower Accumulation of Fe oxides (ferrihydrite ) around bacterial cells collected from a deep water... Fig. 17.8 Upper Bacterial relics filled with ferri-hydrite, probably from Lepthotrix (left) and Gal-lionella (right), formed by rapid oxidation offerri-ferrous waters of drainage ditches (Susser, Schwertmann, 1983 with permission). Lower Accumulation of Fe oxides (ferrihydrite ) around bacterial cells collected from a deep water...
First-order reactions with internal mass-transfer limitations Since the following equation is valid, under the assumption made earlier, we only have to replace the right form of the global rate as expressed in eq. (5.196) ... [Pg.410]

The form of variation of 5/dp for various values of K is shown in Figure 17. The curves are markedly less asymmetric than those produced using the equation derived previously (4), and none of the data discussed there is of the right form to be fitted with Equation 82. [Pg.185]

FIGURE 2 The structure of the globular domain of human PrP in monomeric (left) and dimeric (right) forms. The second subunit is gray to highlight the dramatic conformational change in the green a helix when the dimer is formed. [Pg.150]

B) Space-filling representation of the open (left) and closed (right) forms of the same enzyme.200 Courtesy of Stephen J. Remington. [Pg.702]

Fig. 46. X-Ray structure (left) of the cocrystal of the 1 1 species (right) formed by two complementary components derived from barbituric acid BA (A = ethyl) and 2,4,6-triamino-pyrimidine TAP (B = butyl) [9.119]. Fig. 46. X-Ray structure (left) of the cocrystal of the 1 1 species (right) formed by two complementary components derived from barbituric acid BA (A = ethyl) and 2,4,6-triamino-pyrimidine TAP (B = butyl) [9.119].
Figure 7 3,P and 11B NMR data for the C2-bridged phosphine-boranes 40a-d (top). DFT-optimized structures for 40a (bottom) closed form (left) benefiting from 7t-stacking stabilization, open gauche (middle) and antiperiplanar (right) forms. Figure 7 3,P and 11B NMR data for the C2-bridged phosphine-boranes 40a-d (top). DFT-optimized structures for 40a (bottom) closed form (left) benefiting from 7t-stacking stabilization, open gauche (middle) and antiperiplanar (right) forms.
Figure 27 Optimized structures of the Pd( i-Cl)B-bridging (left) and B-pendant (right) forms of complex 87. ... Figure 27 Optimized structures of the Pd( i-Cl)B-bridging (left) and B-pendant (right) forms of complex 87. ...
Figure 2. Self-complementary base pair between zwitterionic neutral (left) and cationic (right) forms of 7-methylguanine derivatives. Figure 2. Self-complementary base pair between zwitterionic neutral (left) and cationic (right) forms of 7-methylguanine derivatives.
Some expectation values require more complicated integrals. There is a general prescription for determining the correct integral, but here we will merely give the right form for two other important quantities the momentum (p) and the kinetic energy (K) ... [Pg.131]

Fig. 8.3 A molecular muscle in contracted (left) and extended (right) forms [12]... Fig. 8.3 A molecular muscle in contracted (left) and extended (right) forms [12]...
Fig. 4. Reaction sequences of trypsin with normal type and inverse substrates. The hydroxyl function and negative charge represent the catalytic residue (Ser-195) and the binding residue (Asp-189) at the active site, respectively. The acyl trypsin-ligand complex (low right) formed in the presence of a cationic compound... Fig. 4. Reaction sequences of trypsin with normal type and inverse substrates. The hydroxyl function and negative charge represent the catalytic residue (Ser-195) and the binding residue (Asp-189) at the active site, respectively. The acyl trypsin-ligand complex (low right) formed in the presence of a cationic compound...
To get the best out of a catalyst, it has to be deployed in the most appropriate way. The considerations that determine what this should be are shown in the Catalytic Cycle (Figure 1.4). Reactants in the fluid phase have first to be brought to the neighbourhood of the surface, where they must find an active centre where they can be chemisorbed in the right form and with... [Pg.6]

Methylbenzene, also called toluene (presence of methyl group is implied by single bond in the far right form)... [Pg.29]

P-O- H-O-C and P-O- H-O-P hydrogen bond distance in l (left) and dl (right) forms of O-phosphorylated amino acids. (B) 31P chemical shielding tensor orientation in O-phosphorylated amino acids showing three orthogonal projections of the phosphate group hydrogen bond in tyrosine. Taken from Ref. [36],... [Pg.57]

Fig. 11. Schematic diagrams of the open (left) and closed (right) forms, shown for the N-lobe of human lactoferrin. In the conformational change, helix 5 in domain N2 appears to pivot on helix 11. The hinge in the two backbone strands (at Thr 90 and Pro 251) is indicated with an arrow. Taken from Anderson et al. (80). Fig. 11. Schematic diagrams of the open (left) and closed (right) forms, shown for the N-lobe of human lactoferrin. In the conformational change, helix 5 in domain N2 appears to pivot on helix 11. The hinge in the two backbone strands (at Thr 90 and Pro 251) is indicated with an arrow. Taken from Anderson et al. (80).
The key practical problems for the chocolate maker and for the process engineer are that the thermodynamically stable form (Form VI) is not the one that the consumer finds attractive, and that the lower forms will not effectively demould, causing problems in manufacture. Making commercial chocolate thus involves ensuring that the final product is in form V, the right form to be sold and eaten. Figure 22.1 shows... [Pg.527]

Fig. 3.21 Non-polar valence bond (at left) and zwitterionic full charge transfer (at right) forms of a donor-acceptor substituted polyene. Fig. 3.21 Non-polar valence bond (at left) and zwitterionic full charge transfer (at right) forms of a donor-acceptor substituted polyene.

See other pages where Right form is mentioned: [Pg.244]    [Pg.178]    [Pg.173]    [Pg.6]    [Pg.351]    [Pg.351]    [Pg.78]    [Pg.100]    [Pg.383]    [Pg.146]    [Pg.149]    [Pg.136]    [Pg.64]    [Pg.14]    [Pg.30]    [Pg.34]    [Pg.199]    [Pg.178]    [Pg.205]    [Pg.307]    [Pg.462]    [Pg.578]    [Pg.157]   
See also in sourсe #XX -- [ Pg.282 ]

See also in sourсe #XX -- [ Pg.14 ]




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DNA, forms right-handed helical structure

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