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NotesBiology HLTopic 2.2Effect of polar and non-polar amino acids on tertiary structure
Back to Biology HL Topics
2.2.104 min read

Effect of polar and non-polar amino acids on tertiary structure (Biology HL)

IB Biology · Unit 2

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Contents

  1. 1Soluble proteins: polar outside, non-polar core
  2. 2Integral proteins in membranes
  3. 3Exam-style question (step by step)
The big idea: A chain folds so that each R-group ends up where it is most stable: non-polar ones away from water, polar ones in contact with it.

The points to remember

  • In a soluble globular protein, the chain folds so non-polar R-groups cluster in the core.
  • Polar R-groups end up on the surface, where they form hydrogen bonds with water.
  • That is why such proteins dissolve in water: in blood plasma or in the cytoplasm.
  • The hydrophobic core also helps hold the fold together.
Remember it as: Oil in the middle, water-lovers on the skin.
Left: a globular protein with polar R-groups on its surface bonded to water molecules and non-polar R-groups clustered in its core. Right: an integral protein crossing a phospholipid bilayer, its middle region non-polar beside the tails and its two ends polar, facing water
Where polar and non-polar R-groups end up.
Real example: myoglobin: Myoglobin, the oxygen store in muscle, has almost all its non-polar R-groups on the inside and its polar R-groups on the outside, so it dissolves in the watery cytoplasm of muscle cells.

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The big idea: A membrane is the opposite of water inside: its middle is hydrophobic. Proteins that sit in it have a matching hydrophobic belt.

The points to remember

  • An integral protein is embedded in a membrane, crossing the phospholipid bilayer.
  • The part inside the membrane has non-polar R-groups, in contact with the hydrophobic fatty acid tails.
  • The parts outside have polar R-groups, in contact with water on each side.
  • So hydrophobic regions hold the protein in the membrane, the way the core holds a soluble protein together.
Remember it as: A non-polar belt for the tails, polar ends for the water.

Soluble globular protein

  • Non-polar R-groups in the core
  • Polar R-groups on the surface
  • Dissolves in water

Integral membrane protein

  • Non-polar R-groups where it crosses the membrane
  • Polar R-groups at the ends
  • Stays embedded in the bilayer
Real example: aquaporins: Aquaporins, the water channels in kidney cells, cross the membrane several times. Each crossing has a band of non-polar R-groups that sits among the fatty acid tails.

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How it is asked: Paper 1A gives a protein whose polar and non-polar R-groups are placed, and asks what can be deduced. Paper 2 can ask how integral proteins stay in the membrane.
IB-style questionDeduce[1 mark]

In a globular protein, nearly all the non-polar R-groups point inwards and the polar R-groups are on the outside. What can be deduced?

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And a three-mark Explain on integral proteins:

IB-style questionExplain[3 marks]

Explain how the distribution of amino acids allows an integral protein to stay embedded in a membrane.

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where the hydrophobic amino acids are found in a protein that is soluble in water. [1 mark]

Related Biology HL Topics

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2.1.1Chemical properties of carbon that allow diverse compounds2.1.2Production of macromolecules by condensation reactions2.1.3Digestion of polymers into monomers by hydrolysis reactions2.1.4Form and function of monosaccharides
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Improve your exam techniqueCommand terms, paper structure, and mark-scheme tips for Biology HL
Previous2.2.9Bonds and interactions that stabilise tertiary structureNextQuaternary structure of non-conjugated and conjugated proteins2.2.11

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