Question detail

Describe the process of zwitterion formation in amino acids.

Try the question, check the answer, then read the explanation to understand the curriculum point.

At a glance

Question

Type

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Style

Topic

Amino acids, proteins and DNA (A-level only)

Question

Describe the process of zwitterion formation in amino acids.

Answer

A zwitterion is formed when an amino acid undergoes proton transfer. The amine group (-NH2) accepts a proton (H+) to become -NH3+, while the carboxylic acid group (-COOH) donates a proton to become -COO-. This results in a molecule that has both a positive and a negative charge, making it a zwitterion.

Explanation

This answer is strong because it clearly outlines the proton transfer process that leads to zwitterion formation, demonstrating an understanding of amino acid structure and behavior in solution. The question tests the student's ability to explain a key concept in amino acid chemistry.

Common mistake

Zwitterion misconception

Students think a zwitterion is a neutral molecule with no internal charges.

Explain that a zwitterion contains both a positively charged ammonium group (–NH₃⁺) and a negatively charged carboxylate group (–COO⁻) on the same amino‑acid, giving a net zero charge but internal charges that must be considered when describing its formation.

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