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2.3.8—Collagen structure

Syllabus
9700–2028–2029
Objective
2.3.8
Level
AS

Collagen chains form a stabilised triple-helix structure

Collagen is a fibrous protein built from three polypeptide chains that wind together as a triple helix, also called a tropocollagen molecule. Its repeated sequence and layered stabilisation make the structure strong and organised.

  • Three-chain assembly: Each polypeptide chain has a helix shape, and three chains are held closely together by hydrogen bonds to form the triple helix.
  • Repetitive sequence: Glycine occurs at about every third position. Its small R group allows the three chains to pack closely inside the helix.
  • Within the helix: Many hydrogen bonds between the chains stabilise the triple-helix arrangement.
  • Between molecules: Parallel triple helices form covalent cross-links between amino-acid R groups, holding collagen molecules together into fibrils.

The sequence supports close packing, close packing enables the three-chain helix, and hydrogen bonds stabilise that helix. Covalent cross-links then connect neighbouring triple helices into larger fibrils, so stability is built at more than one structural level.

Keep the levels distinct: three polypeptide chains form one triple-helix collagen molecule; cross-links between parallel molecules help form fibrils. This card explains collagen structure and stabilisation, while the next card handles the full structure-to-tissue-function account.

ConceptA-Level CAIE Biology AS