A 100 mL of 0.1 M amino acid at pH 1.0, whose pKa for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH w nonitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G. 12 10 8 pH 6 4 2 0 A B 0.5 с D E F 1.5 2 2.5 Equivalents of OH 1. What is the possible identity of the amino acid? [Select] 2. What is the isoelectric point of the amino acid? [Select] 3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select] 4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select] 5. The effective buffering range for the amino acid in the basic region. [Select] G
A 100 mL of 0.1 M amino acid at pH 1.0, whose pKa for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH w nonitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G. 12 10 8 pH 6 4 2 0 A B 0.5 с D E F 1.5 2 2.5 Equivalents of OH 1. What is the possible identity of the amino acid? [Select] 2. What is the isoelectric point of the amino acid? [Select] 3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select] 4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select] 5. The effective buffering range for the amino acid in the basic region. [Select] G
Chapter1: Relative Value, Addition, And Subtraction Of Decimals
Section: Chapter Questions
Problem 39SST
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![A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH was
monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G.
12
10
8
pH 6
4
2
0
A
B
0.5
с
D
E
F
1.5
2
2.5
Equivalents of OH
1. What is the possible identity of the amino acid? [Select]
2. What is the isoelectric point of the amino acid? [Select]
3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select]
4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select]
5. The effective buffering range for the amino acid in the basic region. [Select]
G
3](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F60de6dac-069d-43b3-b08f-175b617e03fc%2F8f5f4511-922c-4d60-967e-2fc4cc9f6678%2Foewpn6_processed.png&w=3840&q=75)
Transcribed Image Text:A 100 mL of 0.1 M amino acid at pH 1.0, whose pka for the carboxyl group is less than the pKa of the R-group, was titrated with NaOH solution. The pH was
monitored, and the results were plotted on a graph, as shown below. The key points in the titration are designated A to G.
12
10
8
pH 6
4
2
0
A
B
0.5
с
D
E
F
1.5
2
2.5
Equivalents of OH
1. What is the possible identity of the amino acid? [Select]
2. What is the isoelectric point of the amino acid? [Select]
3. What is the pka corresponding to the deprotonation of the alpha-amino group? [Select]
4. Region/ point where the amino acid is predominantly present as a (-2)-charged species. [Select]
5. The effective buffering range for the amino acid in the basic region. [Select]
G
3
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