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Pratt plot

Cook et al. (24) also applied the method of Pratt et al. (27) for evaluating cross-reaction. In this procedure the reciprocal of bound radioligand is plotted vs. competitor concentration. This provides a very sensitive test for divergence of standard curves, ivhich may not be observed in the normal standard displacement plot. The Pratt plot showed rapid divergence of all three lines (d, d,l, and /)/ although divergence between d,I and / lines was less than between d,t and d lines (Fig. 3C). [Pg.44]

Some organic compounds can be in solution with water and the mixture may still be a flammable mixture. The vapors above these mixtures such as ethanol, methanol, or acetone can form flammable mixtures with air. Bodurtha [39] and Albaugh and Pratt [47] discuss the use of Raoult s law (activity coefficients) in evaluating the effects. Figures 7-52A and B illustrate the vapor-liquid data for ethyl alcohol and the flash point of various concentrations, the shaded area of flammability limits, and the UEL. Note that some of the plots are calculated and bear experimental data verification. [Pg.496]

Pratt 80 1 gives several plots of pco against Lp, as shown in Figure 11.62, where Lp is the liquid rate based on the periphery of the packing, in m3/s m. The periphery is taken as a-1(m3/m2), although this is only correct for geometrical systems such as stacked rings. [Pg.648]

D Voet, J Voet, and C Pratt, Fundamentals of Biochemistry, (1999), John Wiley Sons (New York), pp 281-347 Enzymes and kinetics C Whiteley, Biochem. Educ. 25, 144-146 (1997) Enzyme kinetics W Wood et al, Biochemistiy, A Problems Approach, 2nd ed (1981), Benjamin/Cum-mmgs (San Francisco), pp 144-172 Enzyme kinetics with an introduction to the direct linear plot... [Pg.301]

Figure 1.8 Amino add residue side-chain interactions further restrict free rotation in peptide or polypeptide backbone. Rotational possibilities are defined by allowed values of dihedral angle 4> subtended about N—Co, bond and V subtended about Co,—C(0) bond (left). Theoretically allowed angles are shown in Ramachandran plot (right) together with positions of actual angles found in real protein secondary structures a right-handed a-helix ai. left-handed a-helix parallel/S-sheet f anti-parallel 8-sheet C collagen, Pn helix (see later). (Ramachandran plot from Voet, Voet Pratt, 1999 [Wiley], Fig. 6-6). Figure 1.8 Amino add residue side-chain interactions further restrict free rotation in peptide or polypeptide backbone. Rotational possibilities are defined by allowed values of dihedral angle 4> subtended about N—Co, bond and V subtended about Co,—C(0) bond (left). Theoretically allowed angles are shown in Ramachandran plot (right) together with positions of actual angles found in real protein secondary structures a right-handed a-helix ai. left-handed a-helix parallel/S-sheet f anti-parallel 8-sheet C collagen, Pn helix (see later). (Ramachandran plot from Voet, Voet Pratt, 1999 [Wiley], Fig. 6-6).
There are two ways of assessing the shape of a pore (Anderson and Pratt, 1985). One way is to investigate the shape of the hysteresis loop, and the other way is the shape of the amount adsorbed plotted against t. [Pg.142]

The value function is plotted in Figure 2.2.4 against Xif. As has been pointed out (Pratt, 1967), a zero value for Va(x = 0.5) is reasonable, especially for nonisotopic mixtures. This is because the mixture is in the lowest energy state and will require the largest energy for separation (see Chapter 10). See Cohen (1951), Benedict et al. (1981, chap. 12) and Pratt (1967) for detailed treatments on separative power, value functions, etc. for isotope separation plants. [Pg.50]


See other pages where Pratt plot is mentioned: [Pg.18]    [Pg.740]    [Pg.128]    [Pg.167]    [Pg.3601]    [Pg.3603]    [Pg.45]    [Pg.156]    [Pg.186]    [Pg.266]    [Pg.58]    [Pg.581]   
See also in sourсe #XX -- [ Pg.44 , Pg.45 ]




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