Draw aspartic acid (aspartate) at ph 1, ph 7, and ph 13. include hydrogen atoms.
The Correct Answer and Explanation is:

The image above shows the molecular structure of aspartic acid (aspartate) at three different pH levels (pH 1, pH 7, and pH 13). Here’s an explanation of what happens to aspartic acid at each pH:
- At pH 1 (acidic conditions): Aspartic acid has a fully protonated amino group (NH₃⁺) and both carboxyl groups are in their protonated (COOH) form. In acidic conditions, the amino group readily gains a proton (H⁺), resulting in a positively charged NH₃⁺. The carboxyl groups, which typically ionize in more neutral conditions, remain protonated (COOH) and do not carry a negative charge in this acidic environment.
- At pH 7 (neutral conditions): At physiological pH, one carboxyl group (COOH) loses a proton (H⁺), resulting in a negatively charged carboxylate group (COO⁻), while the other carboxyl group remains protonated. The amino group (NH₃⁺) is deprotonated to form NH₂, which is neutral. This form of aspartic acid, with a neutral amino group and a negatively charged carboxyl group, is commonly found in biological systems.
- At pH 13 (basic conditions): In highly basic conditions, both carboxyl groups are deprotonated, resulting in two negatively charged carboxylate groups (COO⁻). The amino group remains neutral (NH₂) because it does not accept a proton in these conditions. This form of aspartic acid is fully deprotonated and has a net negative charge due to the two carboxyl groups.
The ionization states of aspartic acid vary with pH, reflecting the acid-base properties of its functional groups, and these changes are critical for its role in biological systems, including protein structure and enzyme activity.