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The figure below shows the titration curve for the amino acid aspartic acid. There are five key points in the titration designated with roman numerals. For each of the statements following the figure, identify the appropriate key point of the titration

The figure below shows the titration curve for the amino acid aspartic acid. There are five key points in the titration designated with roman numerals. For each of the statements following the figure, identify the appropriate key point of the titration

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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The figure below shows the titration curve for the amino acid aspartic acid. There are five key points in the titration designated with roman numerals. For each of the statements following the figure, identify the appropriate key point of the titration
### Titration Curve Analysis **Graph Explanation:** The graph depicts a titration curve that illustrates the relationship between pH and the equivalents of OH⁻ added. It is divided into five distinct regions labeled I to V. - **X-axis:** Represents the equivalents of OH⁻ added, ranging from 0 to 3.0. - **Y-axis:** Represents the pH levels, ranging from 0 to 14. **Key Points on the Graph:** - **Region I:** Rapid increase in pH as OH⁻ is added. - **Region II:** pH stabilizes around 2.1. - **Region III:** Gradual increase in pH, with a midpoint at pH 3.0. - **Region IV:** Sharp increase in pH, indicating the equivalence point around pH 3.9. - **Region V:** Leveling off of the curve as the solution becomes more basic. **Annotations on the Graph:** - **pH 2.1** is identified as the \( pK_a \) of the α carboxylate. - **pH 3.0** and **pH 3.9** are noted without specific labels but indicate key buffering regions. **Textual Annotations:** 1. **pH is the \( pK_a \) of the α carboxylate.** 2. **pH is the \( pK_a \) of the amine group.** 3. **Average net charge of aspartate is -2.** 4. **Average net charge of aspartate is +1.** 5. **Average net charge of aspartate is 0.** This curve typically represents the titration of an amino acid like aspartate, where the charge transitions are marked at specific \( pK_a \) values, illustrating the changes in net charge as the pH increases.
Transcribed Image Text:### Titration Curve Analysis **Graph Explanation:** The graph depicts a titration curve that illustrates the relationship between pH and the equivalents of OH⁻ added. It is divided into five distinct regions labeled I to V. - **X-axis:** Represents the equivalents of OH⁻ added, ranging from 0 to 3.0. - **Y-axis:** Represents the pH levels, ranging from 0 to 14. **Key Points on the Graph:** - **Region I:** Rapid increase in pH as OH⁻ is added. - **Region II:** pH stabilizes around 2.1. - **Region III:** Gradual increase in pH, with a midpoint at pH 3.0. - **Region IV:** Sharp increase in pH, indicating the equivalence point around pH 3.9. - **Region V:** Leveling off of the curve as the solution becomes more basic. **Annotations on the Graph:** - **pH 2.1** is identified as the \( pK_a \) of the α carboxylate. - **pH 3.0** and **pH 3.9** are noted without specific labels but indicate key buffering regions. **Textual Annotations:** 1. **pH is the \( pK_a \) of the α carboxylate.** 2. **pH is the \( pK_a \) of the amine group.** 3. **Average net charge of aspartate is -2.** 4. **Average net charge of aspartate is +1.** 5. **Average net charge of aspartate is 0.** This curve typically represents the titration of an amino acid like aspartate, where the charge transitions are marked at specific \( pK_a \) values, illustrating the changes in net charge as the pH increases.
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