Amino acids ionization constants

Your body contains a large number of acids, which serve a wide variety of functions. Included are 20 different kinds of amino acids, which are linked to form proteins and the nucleic acid DNA, which stores genetic information. Look up the acid ionization constants of amino acids and DNA. How do the strengths of these acids compare with those of the acids you studied in this activity ... 

The effect of changing pH is different in the two examples given. With alanylglycine the degree of synthesis increases progressively on either side of pH 6, whereas with benzoyltyrosylglycineamide it decreases. The reason is that in the first case the product is a zwitterion whose acid ionization constant is less, and whose basic ionization constant is about twenty-five times stronger, than that of either of its constituent amino acids. 

It can be seen from Table 2 that the intrinsic values of the pK s are close to the model compound value that we use for Cys(8.3), and that interactions with surrounding titratable residues are responsible for the final apparent values of the ionization constants. It can also be seen that the best agreement with the experimental value is obtained for the YPT structure suplemented with the 27 N-terminal amino acids, although both the original YPT structure and the one with the crystal water molecule give values close to the experimentally determined one. Minimization, however, makes the agreement worse, probably because it w s done without the presence of any solvent molecules, which are important for the residues on the surface of the protein. For the YTS structure, which refers to the protein crystallized with an SO4 ion, the results with and without the ion included in the calculations, arc far from the experimental value. This may indicate that con-... 

Chemical Properties. Hydrogen cyanide is a weak acid its ionization constant is of the same magnitude as that of the natural amino acids (qv). Its stmcture is that of a linear, triply bonded molecule, HC=N. 

None of the other reactions so far discussed involve interaction between a pair of charged species. This is but another instance of the electrostatic effect shown by Kirkwood and Westheimer to be responsible for the disparity between the first and second ionization constants of dibasic acids, for the effect of the carboxylate ion on the basicity of an a-amino acid, and for the difference in reactivity of ionic compounds compared with analogous nonionic species in acid- or base-catalyzed reactions. ... 

The titration curve of penicillamine hydrochloride at 25 °C revealed the presence of three ionizable groups with pKa values of 1.8 (carboxyl group), 7.9 (oc-amino group), and 10.5 (/J-thiol group). Recently, the ionization constants for the acidic functions of (D)-penicillamine were verified by pH titration at 37 °C and 0.15 M ionic strength [2], A 1% solution in water has a pH of 4.5-5.5 [3],... 

When the R group contains another ionizable group, the amino acid will have more than two dissociation constants. The carboxylic acid gronps of aspartic acid and glutamic acid, the amine of lysine, and the guanidino group of arginine will all... 

The isoelectric point is equal to the average of the two pRa values for the amino acid. For example, for a generic amino acid (HA), we can write two ionization equilibria and the corresponding equilibrium constant expressions. 

The peptides, which are composed of only a few amino acids, exhibit predictable behavior in CZE in that their mobility (electrophoretic migration) can be predicted on the basis of their size (mass) and their charge characteristics. The charge of such peptides can be predicted from the pKa values of individual amino acids contained in them. For larger peptides and proteins, the calculation of charge based on ionization constant is not trivial and can not be easily calculated based on the pKas of the free amino aids. Besides the mass-to-charge ratio, the other factors that affect mobility are hydrophobic-ity, primary sequence, conformational difference, and the chirality of amino acids. This point has been demonstrated by an investigation on several nonapeptides of identical composition but with different primary sequences ... 

Hydrogen ion titration curves of proteins provide a powerful tool to reveal many aspects of the structures of individual proteins. The characteristic ionization constants of the acidic and basic groups in the amino acids and peptides may be profoundly modified when these groups are incorporated in a protein molecule. An increasing number of proteins have been found in which potentially reactive groups are inaccessible for titration in the native molecule, and become available only after denaturation. Such findings can, in the years ahead, be correlated with detailed knowledge of the three dimensional structure of proteins, as obtained by X-ray diffraction and other methods. The present state of the field is reviewed by Tanford, who has done so much to advance it over the last decade. 

Histidine participation in catalysis was suggested originally by the pH dependence shown in hydrolyses of simple, neutral substrates such as the methyl ester of an N-benzoyl amino acid. The hydrolysis rate typically increases from nearly zero at pH 5 to a maximum value at pH 8. The rate of change is consistent with that of a catalytic process whose rate-limiting step depends on an ionization with an apparent acid dissociation constant, pKa, close to 7. This is a typical value for the dissociation of a proton from a protonated imidazole group ... 

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