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Thus, only the region from pH 1-5 to 6-5 in Fig. 3 remains invariant when the titration curve is determined at various temperatures. e. to give the composition with respect to dissociable amino acid residues. The values obtained in this way agree well with the composition determined using refined analytical techniques on protein hydrolysates. The state of charge of the protein, at any chosen pH value, may also be obtained from the titration curve, by considering the ionization of each group and then computing the net charge.
It is customary to plot pcH against the percentage neutralized (or titrated) at constant volume, although a pH meter would record paH in almost all practical instances. Such curves are of considerable value in deciding upon the correct indicator for use with the analytical determination of acid, or salt concentrations (see Vol. 6). They are also important in connection with buffer systems (see later). Strong acids. g. H+ + Cl- + Na+ + O H " ^ N a + + Cl" + H 2 0. At any stage during the neutralization, but before the equivalence point is reached, the pcH of the system will be determined by the concentration of hydrogen ions that is present.
E. cH+ (and hence pcH) is determined by K and C only. Consider, for example, solutions of acetic acid, for which at 25°C, K = 1-78 x 10~5. The following values of pcH are computed : C = 0-001 moles/1. 001 01 10 pcH == 3-90 3-38 2-88 2-375 As with a strong acid, the acidity rises with increase in concentration, but the 1-0 molar solution contains only about 4 x 10~3g-ions/l. of H+ and an identical concentration of acetate ions. These are the only ions which cause / to deviate from unity, and in this instance the deviation corresponds to 0-032 pH units, so that paH = 2-407.