Draw the predominant form of Gly-Gly when 2.0 moles of OH- is added.

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
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**Question: Draw the predominant form of Gly-Gly when 2.0 moles of OH⁻ is added.**

In this exercise, you are asked to determine and draw the predominant form of the dipeptide Glycylglycine (Gly-Gly) upon addition of 2.0 moles of hydroxide ions (OH⁻).

To solve this problem, one must consider the chemical structure of Gly-Gly and the effect of adding hydroxide ions. Hydroxide ions will likely deprotonate the amino and carboxyl groups in the peptide sequence. 

- **Gly-Gly Structure:**
  - Glycine (Gly) has the side chain -H.
  - In dipeptide form, two glycine molecules are linked by a peptide bond (CONH).

The addition of OH⁻ typically results in the deprotonation of acidic protons:

1. Carboxyl (-COOH) group deprotonation leading to -COO⁻.
2. Amino (-NH₃⁺) deprotonation leading to -NH₂.

Since 2.0 moles of OH⁻ are added, this sufficient quantity will fully deprotonate the available acidic protons in Gly-Gly.

**Detailed Steps to Draw the Predominant Form:**
1. Begin with the Gly-Gly structure:
   ```
      NH3⁺-CH2-CO-NH-CH2-COOH
   ```
2. Identify the groups that can be deprotonated by OH⁻ action:
   - The NH3⁺ group can lose a proton to become NH2.
   - The COOH group can lose a proton to become COO⁻.

3. Upon addition of 2.0 moles of OH⁻, proton distribution will lead to:
   ```
      NH2-CH2-CO-NH-CH2-COO⁻
   ```

So, the predominant form should be represented as the structure provided above. This analysis helps understand the biochemical interactions in a basic environment where Gly-Gly is adjusted with a strong base like OH⁻.
Transcribed Image Text:**Question: Draw the predominant form of Gly-Gly when 2.0 moles of OH⁻ is added.** In this exercise, you are asked to determine and draw the predominant form of the dipeptide Glycylglycine (Gly-Gly) upon addition of 2.0 moles of hydroxide ions (OH⁻). To solve this problem, one must consider the chemical structure of Gly-Gly and the effect of adding hydroxide ions. Hydroxide ions will likely deprotonate the amino and carboxyl groups in the peptide sequence. - **Gly-Gly Structure:** - Glycine (Gly) has the side chain -H. - In dipeptide form, two glycine molecules are linked by a peptide bond (CONH). The addition of OH⁻ typically results in the deprotonation of acidic protons: 1. Carboxyl (-COOH) group deprotonation leading to -COO⁻. 2. Amino (-NH₃⁺) deprotonation leading to -NH₂. Since 2.0 moles of OH⁻ are added, this sufficient quantity will fully deprotonate the available acidic protons in Gly-Gly. **Detailed Steps to Draw the Predominant Form:** 1. Begin with the Gly-Gly structure: ``` NH3⁺-CH2-CO-NH-CH2-COOH ``` 2. Identify the groups that can be deprotonated by OH⁻ action: - The NH3⁺ group can lose a proton to become NH2. - The COOH group can lose a proton to become COO⁻. 3. Upon addition of 2.0 moles of OH⁻, proton distribution will lead to: ``` NH2-CH2-CO-NH-CH2-COO⁻ ``` So, the predominant form should be represented as the structure provided above. This analysis helps understand the biochemical interactions in a basic environment where Gly-Gly is adjusted with a strong base like OH⁻.
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