The big idea: Some proteins are more than one folded chain. How the chains fit together is the quaternary structure.
The points to remember
- Quaternary structure: two or more polypeptide chains held together as one protein.
- Insulin: two chains joined by disulfide bonds.
- Collagen: three chains wound together into a triple helix.
- Haemoglobin: four chains, two alpha and two beta.
Remember it as: Insulin 2, collagen 3, haemoglobin 4.
Not every protein has it: A protein made of one chain, like myoglobin, has no quaternary structure: its highest level is tertiary.
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The big idea: Some proteins need a non-protein partner to work. Haemoglobin cannot carry oxygen without its haem groups.
The points to remember
- A non-conjugated protein is made of polypeptide chains only: insulin, collagen.
- A conjugated protein also has a non-protein part, a prosthetic group.
- Haemoglobin is conjugated: each of its four chains carries a haem group containing iron, which binds oxygen.
- Cryo-electron microscopy freezes molecules and images them, so single proteins can now be seen.
Remember it as: Conjugated = protein + a non-protein part.
Non-conjugated
- Polypeptide chains only
- Insulin: 2 chains
- Collagen: 3 chains
Conjugated
- Chains + a prosthetic group
- Haemoglobin: 4 chains
- + 4 haem groups with iron
Real example: seeing single proteins: Cryo-electron microscopy earned the 2017 Nobel Prize in Chemistry. It has shown the shapes of proteins such as the spike protein of the virus that causes COVID-19.
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How it is asked: A three-mark Outline of the structure of haemoglobin, and a Paper 1A conclusion from a diagram of insulin's chains.
Outline the structure of a haemoglobin molecule.
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And a Paper 1A conclusion from a diagram:
A diagram shows insulin as two chains of amino acids linked by S-S bonds. What can be concluded?
Model answer plan
See the answer broken into clear points, with guidance on how each point earns marks.