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How do amino acids behave in alkaline solutions?

Published in Biochemistry 2 mins read

In alkaline solutions, amino acids act as acids, donating a proton (H+) from their carboxyl group (-COOH).

Detailed Explanation

Amino acids possess both an acidic carboxyl group (-COOH) and a basic amino group (-NH2). This amphoteric nature allows them to behave as either acids or bases depending on the pH of the solution.

Behavior in Alkaline Conditions

  • Deprotonation of the Carboxyl Group: In an alkaline (high pH) environment, the concentration of hydroxide ions (OH-) is high. These hydroxide ions react with the carboxyl group of the amino acid, leading to the removal (deprotonation) of a proton (H+).

    • -COOH + OH- --> -COO- + H2O
  • Formation of a Negatively Charged Ion: The deprotonation of the carboxyl group results in the formation of a negatively charged carboxylate ion (-COO-).

  • Amino Group Remains Mostly Unchanged: While the amino group could theoretically be deprotonated at extremely high pH levels, under typical alkaline conditions, it remains largely protonated (-NH3+).

Summary of Changes

Feature Before (Neutral/Acidic) After (Alkaline)
Carboxyl Group -COOH -COO-
Amino Group -NH3+ -NH3+ (mostly)
Overall Charge Depends on pH Negative

Acting as an Acid

The ability of the amino acid to donate a proton from its carboxyl group in the presence of a base (like hydroxide ions in an alkaline solution) demonstrates its acidic behavior. The amino acid is effectively neutralizing the base by providing a proton.

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