This A-Level Biology Proteins Lesson (AQA Specification 3.1.4.1) provides a 1-hour interactive session focused on protein structure and function. Students will explore amino acids as the building blocks of proteins, learning how they form peptide bonds through condensation reactions. The lesson covers the four levels of protein structure (primary, secondary, tertiary, and quaternary) and explains their biological significance, including enzyme function, transport, and structural roles. The session also includes a practical explanation of the Biuret test for proteins, as well as engaging activities and exam-style questions to test knowledge.
Key Highlights:
Detailed PowerPoint presentation
Learning objectives aligned with AQA specification
Knowledge recall and exam-style questions
Visual diagrams and practical examples
Learning objectives:
Explain how amino acids are linked to form polypeptides – the primary structure of proteins.
Explain how polypeptides are arranged to form the secondary structure and then the tertiary structure of a protein.
Explain how the quaternary structure of a protein is formed.
Describe the test for proteins.
A-Level Biology: Enzyme Action (AQA 3.1.4.2)
This engaging 1-hour lesson covers the key concepts of enzyme action as outlined in the AQA A-Level Biology specification 3.1.4.2. Students will explore how enzymes speed up chemical reactions, understand enzyme specificity through the lock-and-key and induced-fit models, and learn about factors affecting enzyme activity. The lesson includes interactive tasks, such as an enzyme bingo game, and exam-style questions to assess student understanding.
Learning Objectives:
Explain how enzymes speed up chemical reactions.
Describe how enzyme structure relates to function.
Explain the lock-and-key and induced-fit models of enzyme action.
Understand the Biuret test for detecting proteins.
The lesson includes a PowerPoint, tasks with answers, and teacher notes to ensure comprehensive understanding.
This 1-hour lesson covers competitive and non-competitive enzyme inhibition, with engaging tasks and exam-style questions. Students will understand how inhibitors affect enzyme activity, explore feedback inhibition in metabolic pathways, and learn real-world applications of enzyme inhibitors in medicine and industry. The lesson includes knowledge recall, tasks with answers, and a plenary quiz to reinforce key concepts.
Learning Objectives:
Describe the nature of enzyme inhibition.
Explain how competitive and non-competitive inhibitors affect the active site.
Understand the role of feedback inhibition in metabolic pathways.
Introduction to Biological Molecules
Overview of biological molecules and bonding basics.
Spec No: 3.1.1
Monomers and Polymers
Introduction to monomers and polymerization.
Spec No: 3.1.1.1
Carbohydrates: Monosaccharides
Structure and function of glucose and other monosaccharides.
Spec No: 3.1.2
Carbohydrates: Disaccharides and Polysaccharides
Formation of disaccharides and polysaccharides; tests for carbohydrates.
Spec No: 3.1.2
Lipids: Triglycerides and Phospholipids
Structure, function, and formation of lipids.
Spec No: 3.1.3
Proteins: Amino Acids and Peptide Bonds
Structure and properties of amino acids; peptide bonding.
Spec No: 3.1.4
Proteins: Levels of Structure
Primary to quaternary structures of proteins.
Spec No: 3.1.4
Enzymes: Introduction to Enzyme Action
Basic concepts of enzyme structure and function.
Spec No: 3.1.4.2
Enzymes: Factors Affecting Enzyme Activity
Exploring temperature, pH, and substrate concentration on enzymes.
Spec No: 3.1.4.2
Required Practical 1 (RP1): Investigating the Effect of Temperature on Enzyme Activity
Practical focusing on trypsin and temperature effects.