Lesson Plan

• Describe the four hierarchical levels of protein structure and their defining features.
• Explain how hydrogen bonding, hydrophobic interactions, ionic bonds, disulfide bridges and van der Waals forces shape secondary, tertiary and quaternary structures.
• Analyze how a mutation in the primary sequence can alter higher‑order structures and protein function.
• Compare real‑world examples (e.g., hemoglobin, myoglobin, keratin) that illustrate each structural level.

• Projector or interactive whiteboard
• PowerPoint slides with protein‑structure diagrams
• Handout summarising the four levels and key interactions
• 3‑D protein model kits or printable models
• Whiteboard and markers
• Exit‑ticket cards for the conclusion

Begin with a quick “What does a protein look like?” image to spark curiosity. Review that students already know amino acids and peptide bonds from previous lessons. State that by the end of the lesson they will be able to identify and explain each structural level of a protein.

1. Do‑now (5'): Label a short amino‑acid sequence on a worksheet to recall primary structure.
2. Mini‑lecture with slides (10'): Define primary and secondary structures; show α‑helix and β‑sheet diagrams.
3. Guided activity (12'): In small groups, use model kits to build α‑helices and β‑sheets; teacher checks understanding.
4. Interactive demonstration (8'): Discuss forces shaping tertiary structure; manipulate a 3‑D model to illustrate folding.
5. Whole‑class discussion (8'): Introduce quaternary structure using hemoglobin as an example; compare subunit assembly.
6. Formative check (5'): Quick Kahoot quiz or exit‑ticket question asking students to match definitions to each structural level.

Summarise how each level builds on the previous one and why the three‑dimensional shape is crucial for function. Collect exit tickets where students write one example of a protein and identify its structural level. Assign a short homework: create a labelled diagram of a protein showing all four levels.