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a. Why is the pKaof the glutamate side chain greater than the pKaof the aspartate side chain?

b. Why is the pKa of the arginine side chain greater than the pKa of the lysine side chain?

Short Answer

Expert verified

a. The pKaof the glutamate side chain greater than the pKaof the aspartate side chain because the carboxyl group of the aspartic acid side chain is stronger acid than carboxyl group of the glutamic acid side chain because carboxyl group of aspartic acid side chain is closer to electron-withdrawing protonated amino group.

b. The pKa of the arginine side chain greater than the pKa of the lysine side chain because the protonated lysine side chain is stronger acid than the protonated arginine side chain due to less of tendency of arginine side chain to lose a proton as its positive charge is delocalized over three nitrogen atoms.

Step by step solution

01

Inductive effect

Inductive effect refers to the process or phenomenon wherein electron clouds in a bond tends to orient themselves toward the more electronegative element involved in the bond, due to which a permanent dipole arises in a given molecule by this unequal sharing of the bonding electrons in the molecule.

Inductive effect can be used in predicting the acidity and basicity of the given compounds. For example, if we take conjugate base of the acid i.e. RCOO-, here if R is electron-withdrawing group the conjugate base is stabilized via delocalization of formal negative charge and increases the acidity of the compound.

If R is electron donating group, then the conjugate base would be destabilize because of interelectronic repulsions, hence acidity decreases and basicity increases in the compound.

02

Identify (a) and (b)

a. The pKa of the glutamate side-chain greater than the pKa of the aspartate side chain because the carboxyl group of the aspartic acid side chain is a stronger acid than the carboxyl group of the glutamic acid side chain because the carboxyl group of the aspartic acid side chain is closer to electron-withdrawing protonated amino group.

b. The pKaof the arginine side chain is greater than the pKaof the lysine side chain because the protonated lysine side chain is a stronger acid than the protonated arginine side chain due to less of the tendency of the arginine side chain to lose a proton as its positive charge is delocalized over three nitrogen atoms.

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Most popular questions from this chapter

a.Which amino acid has the lowest pI value?

b.Which amino acid has the highest pI value?

c.Which amino acid has the greatest amount of negative charge at pH = 6.20?

d.Which amino acid has a greater negative charge at pH = 6.20, glycine or methionine?

After the polypeptide shown below was treated with maleic anhydride, it was hydrolyzed by trypsin. (After a polypeptide is treated with maleic anhydride,

trypsin will cleave the polypeptide only on the C-side of arginine.)

Gly-Ala-Asp-Ala-Leu-Pro-Gly-Ile-Leu-Val-Arg-Asp-Val-Gly-Lys-Val-Glu-Val-Phe-Glu-Ala-Gly-

Arg-Ala-Glu-Phe-Lys-Glu-Pro-Arg-Leu-Val-Met-Lys-Val-Glu-Gly-Arg-Pro-Val-Gly-Ala-Gly-Leu-Trp

a. After a polypeptide is treated with maleic anhydride, why does trypsin no longer cleave it on the C-side of lysine?

b. How many fragments are obtained from the polypeptide?

c. In what order will the fragments be eluted from an anion-exchange column using a buffer of pH = 5?

Glutathione is a tripeptide whose function is to destroy harmful oxidizing agents in the body. Oxidizing agents are bought to be responsible for some of the effects of aging and to play a causative role in cancer.

Glutathione removes oxidizing agents by reducing them. In the process, glutathione is oxidized, resulting in the formation of a disulphide bond between two glutathione molecules. An enzyme subsequently reduces the disulphide bond, returning glutathione to its original condition so it can react with another oxidizing agent.

a. What amino acids make up glutathione?

b. What is unusual about glutathione’s structure?

Draw the form of aspartate that predominates at the following pH values:

a. pH = 1.0 b. pH = 2.6 c. pH = 6.0 d. pH = 11.0

Explain why the pI of lysine is the average of the pKa values of its two protonated amino groups.

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