Universidad Autnoma del Estado de Mxico

Facultad de Qumica
Qumico Farmacutico Bilogo
Bioqumica Bsica
Fecha de entrega: 08/sep/2017

Problemario 2 Propiedades anfotricas de los aminocidos, estructura y

degradacin de protenas

1. Relationship between the Titration Curve and the Acid-Base Properties of Glycine A 100
mL solution of 0.1 M glycine at pH 1.72 was titrated with 2 M NaOH solution. The pH was
monitored and the results were plotted as shown in the following graph. The key points in the
titration are designated I to V. For each of the statements (a) to (o), identify the appropriate key
point in the titration and justify your choice.

Note: before considering statements (a) through (o), refer to Figure 310. The three species
involved in the titration of glycine can be considered in terms of a useful physical analogy. Each
ionic species can be viewed as a different floor of a building, each with a different net charge:
+
H3N-CH2-COOH +1
+
H3N-CH2-COO- (zwitterion)
H2N-CH2-COO- -1

The floors are connected by steep stairways, and each stairway has a landing halfway between the
floors. A titration curve traces the path one would follow between the different floors as the pH
changes in response to added OH-. Recall that the pKa of an acid (on a halfway landing) represents
the pH at which half of the acid is deprotonated. The isoelectric point (pI) is the pH at which the
average net charge is zero. Now you are ready to consider statements (a) through (o).

(a) Glycine is present predominantly as the species +H3N-CH2-COOH.

(b) The average net charge of glycine is +(1/2) .
(c) Half of the amino groups are ionized.
(d) The pH is equal to the pKa of the carboxyl group.
(e) The pH is equal to the pKa of the protonated amino group.
(f) Glycine has its maximum buffering capacity.
(g) The average net charge of glycine is zero.
(h) The carboxyl group has been completely titrated (first equivalence point).
 Universidad Autnoma del Estado de Mxico
Facultad de Qumica
Qumico Farmacutico Bilogo
Bioqumica Bsica
(i) Glycine is completely titrated (second equivalence point).

(j) The predominant species is +H3N-CH2-COO-.

(k) The average net charge of glycine is -1.
(l) Glycine is present predominantly as a 50:50 mixture of +H3N-CH2-COOH and +H3N-CH2-COO-.
(m) This is the isoelectric point.
(n) This is the end of the titration.
(o) These are the worst pH regions for buffering power.

2. Calculate the pH of the alanine solution after the addition of 0ml, 5ml of 0.1M NaOH and
calculate pH after addition of 1ml, 2.5ml of HCl.

3. Calculate the pH of the arginine solution after the addition of 0ml, 5ml of 0.1M NaOH and
calculate pH after addition of 0.5 ml, 2 ml of HCl.

4. At what pH-range did the acid show buffering behaviour? What are the chemical species at that
region, what are their proportions?

5. Draw the fully protonated structure of Alanine

a. Which protons come off when?

i. -COOH (pKa = 2.3) comes off first (has lower pKa)
ii. -NH3 + (pKa = 9.9)
b. Write out structures for sequential deprotonation of Ala in agreement with pKa values.

6. Draw the structures and the equilibria representing the complete deprotonation of the Aspartate
(Asp, D)
a. Determine what the pKas of the titratable protons are by looking at the pKa table.
b. Determine net charge on each ionized form.
c. Find the structure that has no net charge.

7. Draw the PEPTIDE BACKBONE fully protonated for the next many amino acids: ALDRS, N
C-terminus.
a. Determine if groups are ionized at the pH 1.5, 5.0, 7.0, 8.5, 12.
b. Determine net charge on each ionized form.
c. Find the structure that has no net charge.