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NotesBiology HLTopic 2.2Impact of primary structure on the conformation of proteins
Back to Biology HL Topics
2.2.74 min read

Impact of primary structure on the conformation of proteins (Biology HL)

IB Biology · Unit 2

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Contents

  1. 1Sequence decides shape
  2. 2Precise, predictable, repeatable
  3. 3Exam-style question (step by step)
The big idea: A protein's shape is written in its sequence. The order of amino acids decides where each R-group ends up, and so how the chain folds.

The points to remember

  • The primary structure is the sequence of amino acids, set by the gene.
  • In water, the chain folds so hydrophobic R-groups end up inside and hydrophilic ones outside.
  • R-groups that meet form hydrogen bonds, ionic bonds and disulfide bonds that hold the fold.
  • So the sequence, and the precise position of each amino acid, decides the 3-D shape: the conformation.
Remember it as: Sequence → R-group positions → bonds → shape.
A chain of beads of three kinds (hydrophobic, polar, charged) folds so that the hydrophobic beads cluster in a core, polar and charged beads stay outside and a positive and a negative bead form an ionic bond; a second chain with the same sequence folds into the same shape
How the sequence decides the shape.
Real example: human insulin made by bacteria: Bacteria given the human insulin gene make a chain with exactly the human sequence. It folds into the same shape as insulin made in the pancreas, so it works in people with diabetes.

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The big idea: Even very large proteins fold the same way every time, because each amino acid sits in the same place in every copy.

The points to remember

  • The same sequence always folds into the same shape: protein structures are precise, predictable and repeatable.
  • That is why every copy of an enzyme has the same active site.
  • Change one amino acid and its R-group changes, so the bonds and the fold can change.
  • A changed fold can mean a protein that works less well, or not at all.
Remember it as: Same sequence, same shape; new sequence, maybe a new shape.

Same sequence

  • Same R-groups in the same positions
  • Same bonds form
  • Same 3-D shape, same function

One amino acid changed

  • A different R-group at one position
  • Some bonds change
  • The shape and function may change

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How it is asked: A four-mark Explain linking the sequence to the tertiary structure, and questions on what a single change in sequence does.
IB-style questionExplain[4 marks]

After synthesis, globular proteins fold into their final tertiary structure. Explain the relationship between the sequence of amino acids and the tertiary structure.

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And a two-mark Outline on a change in sequence:

IB-style questionOutline[2 marks]

Outline how a change to one amino acid in a protein's sequence can change its function.

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IB Exam Questions on Impact of primary structure on the conformation of proteins

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How Impact of primary structure on the conformation of proteins Appears in IB Exams

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  • Define

    Give the precise meaning of key terms related to Impact of primary structure on the conformation of proteins.

    AO1
  • Describe

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  • Explain

    Give reasons WHY — cause and effect within Impact of primary structure on the conformation of proteins.

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  • Evaluate

    Weigh strengths AND limitations of approaches in Impact of primary structure on the conformation of proteins.

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    Present arguments FOR and AGAINST with a balanced conclusion.

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Related Biology HL Topics

Continue learning with these related topics from the same unit:

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
View all Biology HL topics
Improve your exam techniqueCommand terms, paper structure, and mark-scheme tips for Biology HL
Previous2.2.6Chemical diversity in the R-groups of amino acidsNextPleating and coiling of secondary structure2.2.8

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