Lesson Plan

• Describe the four main types of interactions that stabilise protein structure.
• Explain how each interaction contributes to secondary, tertiary or quaternary structure.
• Compare the relative strength and environmental sensitivity of non‑covalent versus covalent interactions.
• Predict how changes in pH or redox conditions affect protein stability.
• Apply knowledge to interpret a diagram of a folded protein showing these interactions.

• Projector and computer with PowerPoint slides
• Printed handout containing the interaction summary table
• Protein molecular model kits
• Whiteboard and markers
• Kahoot quiz access (or similar) for formative check
• Exit‑ticket cards for the conclusion

Begin with a quick image of a folded protein and ask students what keeps it in that shape. Review prior knowledge that proteins are polymers of amino acids that must fold to function. State that by the end of the lesson they will be able to identify and explain the five key interactions that stabilise protein structure.

1. Do‑now (5'): short quiz on basic protein terminology and primary structure.
2. Mini‑lecture with slides (15'): introduce hydrophobic, hydrogen, ionic, and disulfide interactions, using examples from the source.
3. Model activity (10'): students build a simple protein using kits and label where each interaction occurs.
4. Guided worksheet (10'): analyse a provided diagram and answer questions about the role of each interaction.
5. Think‑pair‑share (5'): discuss how pH changes would affect ionic (salt‑bridge) interactions.
6. Formative check (5'): Kahoot quiz to confirm understanding of strengths and locations of each interaction.

Recap the five interactions and their contributions to protein stability. Students complete an exit‑ticket stating one real‑world example of a protein whose function depends on a specific interaction. Assign homework: read a short case study on disulfide‑bonded antibodies and prepare a one‑paragraph summary.