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Total acid number, defined

Free and total acid are defined as the number of milliliters of 0.1 M NaOH needed to reach the first and second endpoint, respectively. [Pg.465]

Acidity is determined through the acid number, which is the quantity of base, expressed in milligrams of potassium hydroxide per gram of sample, required to titrate a sample in the solvent from its initial meter reading to a meter reading corresponding to a freshly prepared nonaqueous basic buffer solution or a well-defined inflection point as specified in the test method. Test methods include potentiometric titration (ASTM D-66, IP 177) and indicator-indicator titration (ASTM D-974, IP 139) in addition to inorganic acidity (IP 182) and total acidity (IP 1) methods. [Pg.201]

AN, the acceptor number of Lewis acids, was defined as the relative P NMR shift obtained when triethylphosphine oxide (EtsPO) was dissolved in the eandidate acid. The scale was normalized by assigning an AN value of 0 to the NMR shift obtained with hexane, and 100 to that obtained from the SbCLrEtsPO interaetion in dilute 1,2-dichloroethane solution. However, the total shift of P NMR in two-eomponent systems has an appreciable contribution of van der Waals interactions that must be accounted for in correlating spectral shifts with heats of acid base interactions. Riddle and Fowkes [7] corrected the P NMR shifts for van der Waals interactions and proposed a new scale of acceptor numbers. The new AN values (AN—AN ) in ppm are converted into AN in kcal/mol units by... [Pg.108]

The acid numbers of the oxidates determined by titration with aqueous-alcohol solution of NaOH and indicator phenolphthalein is of an order higher than the content of adipic acid as determined by GC. This observation demonstrates the complex composition of the acids. Ref [97] is considered, however, that the acid number is completely defined by the presence of adipic acid. But this statement obviously contradicts the chromatographic data obtained by us. The latter shows that adipic acid comprises a very small percent of the total acid content. [Pg.411]

An effective method for localizing causes of redox potentials is to plot the total backbone and side chain contributions to ( ) per residue for homologous proteins as functions of the residue number using a consensus sequence, with insertions treated by summing the contribution of the entire insertion as one residue. The results for homologous proteins should be examined for differences in the contributions to ( ) per residue that correlate with observed redox potential differences. These differences can then be correlated with any other sequence-redox potential data for proteins that lack crystal or NMR structures. In addition, any sequences of homologous proteins that lack both redox potentials and structures should be examined, because residues important in defining the redox potential are likely to have semi-sequence conservation of a few key amino acid types. [Pg.407]

Fig. 3-3. Comparison of the values of enantiomeric resolution of different DNP-D,L-amino acids at different deconvolution stages of a cyclic hexapeptide sublibrary. Resolution values in a cyclo(Arg-Lys-X-X-X-P-Ala) sublibrary, in the first line, are compared to those obtained in sublibraries with a progressively increasing number of defined positions. All the sublibraries were 30 mM in the running buffer while the completely defined cyclo(Arg-Lys-Tyr-P-Tyr-P-Ala) peptide is used at 10 mM concentration. Conditions cyclopeptide sublibrary in 20 mM sodium phosphate buffer, pH 7.0 capillary, 50 pm i.d., 65 cm total length, 57 cm to the window V = -20 kV, I = 40 electrokinetic injection, -10 kV, 3 s detection at 340 nm. (Reprinted with permission from ref. [75]. Copyright 1998, American Chemical Society.)... Fig. 3-3. Comparison of the values of enantiomeric resolution of different DNP-D,L-amino acids at different deconvolution stages of a cyclic hexapeptide sublibrary. Resolution values in a cyclo(Arg-Lys-X-X-X-P-Ala) sublibrary, in the first line, are compared to those obtained in sublibraries with a progressively increasing number of defined positions. All the sublibraries were 30 mM in the running buffer while the completely defined cyclo(Arg-Lys-Tyr-P-Tyr-P-Ala) peptide is used at 10 mM concentration. Conditions cyclopeptide sublibrary in 20 mM sodium phosphate buffer, pH 7.0 capillary, 50 pm i.d., 65 cm total length, 57 cm to the window V = -20 kV, I = 40 electrokinetic injection, -10 kV, 3 s detection at 340 nm. (Reprinted with permission from ref. [75]. Copyright 1998, American Chemical Society.)...
By the components of the system we are to understand the least number of independently variable constituents, in terms of which the composition of every phase in the system can be completely specified. The number of components will therefore contribute to the total number of independent variables defining the state of chemical and physical equilibrium of the system. It is not necessary that the components shall be actual constituents of the system all that is required is that they shall be independently variable, Le.y the least number has been chosen. Thus, in systems composed of solid fuming sulphuric acid in presence... [Pg.169]

A large number of other reactions are also possible, e.g., hydration of the various substances, or (if the solute is a salt of a weak acid or base) hydrolysis, but in all cases the concentration of each molecular species is defined by the total amount of solute in a given mass of solution, and the ionisation proceeds as if all the other reactions did not occur at all (cf. 158). [Pg.369]

The first equation defines the ionization constant of water at 25 °C (we omit the sign of the charges to simplify notation). The second is the same as Eq. (2.6.3), while the third is the conservation of the total initial concentration of the (weak) acid Nj- (we assume that there is no change in volume during the titration, hence this is the same as the conservation of the total number of acid molecules). The fourth equation is the electroneutrality condition, where [iV ] is the concentration of the added (strong) base. [Pg.45]

There are two definitions of protein hydrophobicity average hydrophobicity and surface hydrophobicity. The average hydrophobicity was defined by Bigelow (1967) as the total hydrophobicity of all amino acid residues comprising a protein divided by the number of amino acids in the protein. There is no standard definition of surface (or effective) hydrophobicity except the concept that there must be hydrophobic regions on the molecular surface that play an effective role in protein function. Readers who are interested in a more detailed discussion are referred to Nakai and Li-Chan (1988). [Pg.308]


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See also in sourсe #XX -- [ Pg.105 ]




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Acid number

Acidity number

Acids defined

Number, defined

Numbers total

Total acidity

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