Lesson Plan

• Describe the primary, secondary, tertiary and quaternary structural levels of haemoglobin.
• Explain how two α‑globin and two β‑globin chains combine with four haem groups to form the functional tetramer.
• Illustrate the “dimer of dimers” arrangement and its role in cooperative oxygen binding.

• Projector and screen
• PowerPoint/Google Slides with haemoglobin diagrams
• 3‑D printed or paper model of haemoglobin tetramer
• Handout worksheet with labelled diagram
• Whiteboard and markers
• Clicker or Kahoot quiz set‑up

Begin with a quick question: “How does blood deliver oxygen to tissues?” Connect students’ prior knowledge of oxygen transport to the idea that proteins carry out this function. State that today they will uncover how haemoglobin’s structure enables its role, and list the success criteria: identify each structural level, describe subunit composition, and explain cooperative binding.

1. Do‑now (5'): Students complete a short recall quiz on primary‑secondary‑tertiary structures.
2. Mini‑lecture with slides (10'): Overview of protein structural hierarchy, focusing on haemoglobin’s subunits and haem group.
3. 3‑D model exploration (10'): Teacher demonstrates the tetramer using the model; students rotate and identify α‑ and β‑chains and haem pockets.
4. Group activity – “Build the Tetramer” (15'): Teams assemble paper cut‑outs of α, β, and haem pieces, then label each component.
5. Concept‑check clicker questions (5'): Immediate feedback on quaternary assembly and cooperative binding.
6. Guided summary discussion (5'): Reinforce the “dimer of dimers” concept and link structure to function.

Recap the four structural levels and how they culminate in haemoglobin’s tetrameric form that enables oxygen cooperativity. Ask students to write one key takeaway on an exit ticket. For homework, assign the textbook section on globular proteins and a worksheet requiring students to label a haemoglobin diagram.