IB Biology HL B1.2.8 Hl Secondary Structure Questions

Explore how local polypeptide coils and pleats form alpha helices and beta sheets, stabilized by regular backbone hydrogen bonding in IB Biology HL B1.2.8.

Exam points

Identify alpha helices and beta-pleated sheets as local secondary structures in polypeptides.
Explain that regular hydrogen bonds between peptide-group C=O and N-H atoms stabilize secondary structure.
Distinguish secondary-structure hydrogen bonding from tertiary interactions when interpreting protein diagrams or models.

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Study B1.2.8 (HL)—Secondary structure conceptsOpen the corresponding Concept lesson for explanations, examples and exam connections.

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Titin is the longest protein in the human body, consisting of a single strand of over 34000 amino acids.

Figure for Question IB Biology HL B1.2.8 Hl Secondary Structure Questions question 1 — IB Biology HL

Describe the secondary structures represented by the arrows in the diagram.

a. beta/ $\beta$ -pleated sheets;
b. (structure held in place by) hydrogen bonds between N-H and C=O on different amino acids
OR
hydrogen bonds between sections of polypeptide running parallel or antiparallel
OR
sections of polypeptide form a pleat (when they run in opposite directions) because of the tetrahedral bond angles;

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IB Biology HL B1.2.8 Hl Secondary Structure Questions question 1