Skip to content
Dabour HubLEARN · PRACTICE · EXPLORESign inStudent

5.5.7Unit 5. Transition Metals and Organic Nitrogen Chemistry

Characteristic Behaviour of Amino Acids — IAL Edexcel Linear (Chemistry) Revision Notes & Topical Questions

5 min read 5 parts Lesson 37 of 43 Unit quiz

🩺
100% Curriculum Specification Match Lesson Doctor Verified
The only platform with 100% curriculum specification match and verified interactive question banks.
Curriculum Equation Key pH & Acid-Base Equilibrium FormulasFast Exam Solution
pH = -log[H⁺] | pOH = -log[OH⁻] | pH + pOH = 14 | [H⁺][OH⁻] = 10⁻¹⁴
Word Equation & Conditions: pH + pOH = 14
0%read

Part 1 of 5Structure and Zwitterions

5.5.7 Characteristic Behaviour of Amino Acids

Both an acidic and a basic group are present on one molecule.

General structure
  • A 2-amino acid has the formula H₂N–CHR–COOH, with the amine and carboxylic acid groups on the same carbon.
Zwitterion
  • In the solid and in solution near neutral pH, the molecule transfers H⁺ from –COOH to –NH₂, giving ⁺H₃N–CHR–COO⁻.
Physical properties
  • Ionic interactions between zwitterions give high melting points, and most amino acids dissolve in water.
Chirality
  • Every 2-amino acid except glycine has four different groups on the central carbon and so shows optical isomerism.

Part 2 of 5Acid–Base Behaviour

Acid–Base Behaviour
With acid
  • In strongly acidic solution the –COO⁻ group takes up H⁺, giving the cation ⁺H₃N–CHR–COOH.
With alkali
  • In strongly alkaline solution the –NH₃⁺ group loses H⁺, giving the anion H₂N–CHR–COO⁻.
Amphoteric
  • The ability to react as both an acid and a base is called amphoteric behaviour.
Isoelectric point
  • The pH at which the overall charge is zero and the zwitterion predominates;
    • the amino acid does not move in an electric field.
pH of solutionDominant form of glycineOverall charge
Low (strong acid)⁺H₃NCH₂COOH+1
Near isoelectric point⁺H₃NCH₂COO⁻0
High (strong alkali)H₂NCH₂COO⁻–1

Part 3 of 5Reactions of Amino Acids

1
With an alcohol and a few drops of concentrated acid catalyst under reflux, the –COOH group forms an ester, for example the methyl ester of glycine.
2
Two amino acids can join when the –NH₂ of one reacts with the –COOH of another, releasing water to form a dipeptide.
3
Repeating this step builds polypeptides, and the sequence of side groups R decides the final protein structure.
4
Heating a peptide with aqueous acid for many hours hydrolyses every amide link and returns the separate amino acids.
5
Ninhydrin spray on a chromatogram turns the amino acid spots purple so they can be identified by Rf value.

Part 4 of 5Separation and Identification

Electrophoresis
  • At a fixed pH, amino acids move at different rates towards the electrodes depending on their charge and size.
Paper chromatography
  • Amino acids have different solubilities in the solvent, so they travel different distances up the paper.
Rf value
  • Rf equals the distance moved by the spot divided by the distance moved by the solvent front.
Developing agent
  • Ninhydrin is used because the amino acids are colourless on the paper.

Part 5 of 5Exam Checklist & Tips

5.5.7 – Key Points for the Exam

  • 2-Amino acid A molecule with an amine and a carboxylic acid group on the same carbon atom.
  • Zwitterion An ion carrying both a positive and a negative charge with zero overall charge.
  • Amphoteric Able to react both as an acid and as a base.
  • Isoelectric point The pH at which an amino acid has no net charge.
  • Peptide link The amide link formed between two amino acids.

Common Mistakes

  • Drawing amino acids as uncharged H₂N–CHR–COOH in solid or neutral solution rather than as zwitterions.
  • Stating that glycine is chiral; its R group is hydrogen so it has no optical isomer.
  • Saying the isoelectric point is pH 7 for all amino acids; it depends on the side chain.
  • Confusing the cation (low pH) with the anion (high pH) forms.

Last updated:

\n