This lesson describes and explains the effect of an increasing temperature on the rate of an enzyme-catalysed reaction. The PowerPoint and the accompanying resource are part of the 1st lesson in a series of 4 which cover the content detailed in point 3.2 (a) of the CIE A-level Biology specification and this lesson has been specifically planned to tie in with the lesson in 3.1 where the properties of enzymes and their mechanism of action were introduced. The lesson begins by challenging the students to recognise optimum as a key term from its 6 synonyms that are shown on the board. Time is taken to ensure that the students understand that the optimum temperature is the temperature at which the most enzyme-product complexes are produced per second and therefore the temperature at which the rate of an enzyme-controlled reaction works at its maximum. The optimum temperatures of DNA polymerase in humans and in a thermophilic bacteria and RUBISCO in a tomato plant are used to demonstrate how different enzymes have different optimum temperatures and the roles of the latter two in the PCR and photosynthesis are briefly described to prepare students for these lessons in topics 19 and 13. Moving forwards, the rest of the lesson focuses on enzyme activity at temperatures below the optimum and at temperatures above the optimum. Students will understand that increasing the temperature increases the kinetic energy of the enzyme and substrate molecules, and this increases the likelihood of successful collisions and the production of enzyme-substrate and enzyme-product complexes. When considering the effect of increasing the temperature above the optimum, continual references are made to the previous lesson and the control of the shape of the active site by the tertiary structure. Students will be able to describe how the hydrogen and ionic bonds in the tertiary structure are broken by the vibrations associated with higher temperatures and are challenged to complete the graph to show how the rate of reaction decreases to 0 when the enzyme has denatured. Please note that this lesson has been designed specifically to explain the relationship between the change in temperature and the rate of reaction and not the practical skills that would be covered in a core practical lesson

This fully-resourced lesson describes how enzymes function intracellularly and extracellularly and explains their mode of action. The engaging PowerPoint and accompanying resources have been designed to cover points 3.1 (a, b & c) and considers the details of Fischer’s lock and key hypothesis and Koshland’s induced-fit model and explains how an enzyme’s specificity is related to their 3D structure and enables them to act as biological catalysts. The lesson has been planned to tie in with topic 2.3, and to challenge the students on their knowledge of protein structure and globular proteins. This prior knowledge is tested through a series of exam-style questions along with current understanding and mark schemes are included in the PowerPoint so that students can assess their answers. Students will learn that enzymes are large globular proteins which contain an active site that consists of a small number of amino acids. Emil Fischer’s lock and key hypothesis is introduced to enable students to recognise that their specificity is the result of an active site that is complementary in shape to a single type of substrate. Time is taken to discuss key details such as the control of the shape of the active site by the tertiary structure of the protein. The induced-fit model is described so students can understand how the enzyme-susbtrate complex is stabilised and then students are challenged to order the sequence of events in an enzyme-controlled reaction. The lesson finishes with a focus on ATP synthase and DNA polymerase so that students are aware of these important intracellular enzymes when learning about the details of respiration and DNA replication before they are challenged on their knowledge of carbohydrates, lipids and proteins from topics 1.2 - 1.4 as they have to recognise some extracellular digestive enzymes from descriptions of their biological molecule substrates.

This lesson describes and explains how increasing the concentration of inhibitors affects the rate of an enzyme-catalysed reaction. The PowerPoint and accompanying resource are the last in a series of 4 lessons which cover the content detailed in point 3.2 (a) of the CIE A-level Biology specification but this lesson also covers point 3.2 [c] as competitive and non-competitive inhibitors are introduced and their differing effects on enzyme activity described and explained. The lesson begins with a made up round of the quiz show POINTLESS called “Biology opposites” and this allows students to recognise that inhibition is the opposite of stimulation. This introduces inhibitors as substances that reduce the rate of a reaction and students are challenged to use their general knowledge of enzymes to identify that inhibitors prevent the formation of the enzyme-substrate complex. Moving forwards, a quick quiz competition generates the abbreviation EIC (representing enzyme-inhibitor complex) and this introduces competitive inhibitors as substances that occupy the active site. The students are asked to apply their knowledge to a new situation to work out that these inhibitors must have a similar shape to the enzyme’s substrate molecule. A series of exam-style questions are used throughout the lesson and at this point, the students are challenged to work out that an increase in the substrate concentration would reduce the effect of a fixed concentration of a reversible competitive inhibitor. The rest of the lesson focuses on non-competitive inhibitors and time is taken to ensure that key details such as the disruption of the tertiary structure is understood and biological examples are used to increase the relevance. Again, students will learn that increasing the concentration of the inhibitor results in a greater inhibition and a reduced rate of reaction but that increasing the substrate concentration cannot reduce the effect as was observed with competitive inhibitors.

This lesson describes how enzymes can be immobilised in calcium alginate and compares their activity against enzymes that are free in solution. The PowerPoint and the accompanying resources have been designed to cover point 3.2 (d) of the CIE A-level Biology specification. The lesson has been planned to challenge the students on their ability to apply knowledge to a potentially unfamiliar situation. A series of exam-style questions which include “suggest” and “describe and explain” questions are used throughout the lesson and these will allow the students to recognise the advantages and disadvantages of a particular method. Although the alginate method is the only one referenced in this specification point, the adsorption and covalent bonding methods are introduced and then briefly analysed to allow students to understand that a matrix doesn’t involve these bonds which could disrupt the active site. The remainder of the lesson introduces some actual examples of the use of immobilised enzymes with the aim of increasing the relevance. Please note that this lesson has been written to explain the effect of immobilisation on enzyme activity. The practical element of carrying out the investigation is described in a separate lesson.

This lesson describes and explains how increasing the temperature affects the rate of an enzyme-controlled reaction. The PowerPoint and the accompanying resource have been designed to cover the second part of point 1.4.2 of the AQA A-level Biology specification and ties in directly with the previous lesson on the properties of enzymes and their mechanism of action. The lesson begins by challenging the students to recognise optimum as a key term from its 6 synonyms that are shown on the board. Time is taken to ensure that the students understand that the optimum temperature is the temperature at which the most enzyme-product complexes are produced per second and therefore the temperature at which the rate of an enzyme-controlled reaction works at its maximum. The optimum temperatures of DNA polymerase in humans and in a thermophilic bacteria and RUBISCO in a tomato plant are used to demonstrate how different enzymes have different optimum temperatures and the roles of the latter two in the PCR and photosynthesis are briefly described to prepare students for these future lessons. Moving forwards, the rest of the lesson focuses on enzyme activity at temperatures below the optimum and at temperatures above the optimum. Students will understand that increasing the temperature increases the kinetic energy of the enzyme and substrate molecules, and this increases the likelihood of successful collisions and the production of enzyme-substrate and enzyme-product complexes. When considering the effect of increasing the temperature above the optimum, continual references are made to the previous lesson and the control of the shape of the active site by the tertiary structure. Students will be able to describe how the hydrogen and ionic bonds in the tertiary structure are broken by the vibrations associated with higher temperatures and result in an active site that is no longer complementary to the substrate. Key terminology such as denaturation is used throughout. Please note that this lesson has been designed specifically to explain the relationship between the change in temperature and the rate of reaction and not the practical skills that would be covered in a core practical lesson

This detailed lesson describes the the structure and function of the motor neurones that form the autonomic nervous system and is responsible for automatic responses. The engaging PowerPoint and accompanying resource have been designed to cover point 9.4 (v) of the Edexcel A-level Biology B specification and describes the sympathetic and parasympathetic divisions and how they act antagonistically. The lesson begins with a focus on the types of effectors that will be connected to the CNS by autonomic motor neurones. Students will learn that effectors which are not under voluntary control such as cardiac muscle, smooth muscle and glands will be innervated by these neurones. Moving forwards, a quick quiz competition is used to introduced ganglia as a structure which connects the two or more neurones involved in the cell signalling between the CNS and the effector. This leads into the discovery of the two divisions and students will begin to recognise the differences between the sympathetic and parasympathetic systems based on function but also structure. The remainder of the lesson looks at the differing effects of these two systems. This lesson has been written to tie in with the lesson on the organisation of the mammalian nervous system which was covered earlier in this topic

This lesson describes the relationship between the structure and function of a synapse, focusing on acetylcholine as the neurotransmitter. The engaging and detailed PowerPoint and accompanying resources have been designed to cover the content of point 9.5 (iv) of the Edexcel A-level Biology B specification. The lesson begins by using a version of the WALL (as shown in the cover image) which asks the students to group 12 words into three groups of 4. Not only will this challenge their prior knowledge from topics earlier in this topic but it will also lead to the discovery of four of the structures that are found in a synapse. Moving forwards, students are introduced to acetylcholine as the neurotransmitter involved at cholinergic synapses and they will start to add labels to the structures found in the pre-synaptic bulb. Time is taken to focus on certain structures such as the voltage gated channels as these types of channel were met previously when looking at the depolarisation of a neurone. There is plenty of challenge and discovery as students are pushed to explain why organelles like mitochondria would be found in large numbers in the bulb. With this process being a cascade of events, a bullet point format is used to ensure that the key content is taken in by the students and again key points like exocytosis and the action of acetylcholinesterase are discussed further. Understanding checks and prior knowledge checks are included throughout the lesson so that students can not only assess their progress against the current topic but also be challenged to make links to earlier topics.

This lesson introduces the differences between ectotherms and endotherms and then describes the behavioural responses of an ecotherm. The PowerPoint and accompanying resource have been designed to cover specification point 9.9 (vi) of the Edexcel A-level Biology B specification which states that students should understand how ectotherms rely on the external environment for their temperature control. The main aim when designing the lesson was to support students in making sensible and accurate decisions when challenged to explain why these types of organisms have chosen to carry out a particular response. A wide range of animals are used so students are engaged in the content matter and are prepared for the unfamiliar situations that they will encounter in the terminal exam. Time is also taken to compare ectotherms against endotherms so that students can recognise the advantages and disadvantages of ectothermy when covered in the following lesson.

This detailed lesson describes how an endotherm regulates its temperature through behaviour and also physiologically. The engaging PowerPoint and accompanying resources have been designed to cover specification point 9.9 (vii) of the Edexcel A-level Biology B specification and includes descriptions of the roles of the autonomic nervous system, thermoreceptors, hypothalamus and skin. A wide range of activities have been written into this lesson so that students remain motivated throughout and take a genuine interest in the content. Understanding checks allow the students to assess their progress whilst the prior knowledge checks on topics such as enzymes and denaturation demonstrate the importance of being able to make connections and links between topics from across the specification. In addition to these checks, quiz competitions like HAVE an EFFECT which is shown in the cover image are used to introduce key terms and values in a fun and memorable way. The lesson begins by introducing the key term, endotherm, and challenging students to use their prior knowledge and understanding of terminology to suggest what this reveals about an organism. Moving forwards, students will learn how the heat generated by metabolic reactions is used as a source of internal heat. The main part of the lesson focuses on thermoregulation in humans (mammals) and time is taken to focus on the key components, namely the sensory receptors, the thermoregulatory centre in the hypothalamus and the responses brought about by the skin. The important details of why the transfer of heat energy between the body and the environment actually leads to a decrease in temperature are explored and discussed at length to ensure understanding is complete. Students are challenged to write a detailed description of how the body detects and responds to a fall in body temperature and this task is differentiated for those students who need some extra assistance. The peripheral thermoreceptors are introduced and this leads into the final section of the lesson that considers behavioural responses in humans and other animals.

This lesson describes how the mechanisms involved in the selective reabsorption of solutes in the proximal convoluted tubule. The PowerPoint and accompanying resource have been designed to cover the first part of specification point 9.9 (iii) of the Edexcel A-level Biology B specification and builds on the knowledge gained in the previous lessons on the structure of the nephron and ultrafiltration. The lesson begins by challenging the students to recall the substances that are found in the glomerular filtrate so that each of them can be considered over the course of the rest of the lesson. Moving forwards, the first of the numerous discussion points which are included in the lesson is used to get students to predict the component of the filtrate which won’t be found in the urine when they are presented with pie charts from each of these situations. Upon learning that glucose is 100% reabsorbed, along with most of the ions and some of the water, the rest of the lesson focuses on describing the relationship between the structure of the PCT and the function of selective reabsorption. Again, this section begins by encouraging the students to discuss and to predict which structures they would expect to find in a section of the kidney if the function is to reabsorb. They are given the chance to see the structure (as shown in the cover image) before each feature is broken down to explain its importance. Time is taken to look at the role of the cotransporter proteins to explain how this allows glucose, along with sodium ions, to be reabsorbed from the lumen of the PCT into the epithelial cells. The final part of the lesson focuses on urea and how the concentration of this substance increases along the tubule as a result of the reabsorption of some of the water.

This detailed lesson describes the gross and microscopic structure of the mammalian kidney. The engaging PowerPoint and accompanying resource have been designed to cover point 9.9 (i) of the Edexcel A-level Biology B specification. The lesson was designed to tie in with the other lessons in topic 9.9 on ultrafiltration, selective reabsorption and the control of mammalian plasma concentration and a common theme runs throughout to allow students to build their knowledge gradually and develop a deep understanding of this organ. Students will come to recognise the renal cortex and renal medulla as the two regions of the kidney and learn the parts of the nephron which are found in each of these regions. Time is taken to look at the vascular supply of this organ and specifically to explain how the renal artery divides into the afferent arterioles which carry blood towards the glomerulus and the efferent arterioles which carry the blood away. The main task of the lesson challenges the students to relate structure to function. Having been introduced to the names of each of the parts of the nephron, they have to use the details of the structures found at these parts to match the function. For example, they have to make the connection between the microvilli in the PCT as a sign that this part is involved in selective reabsorption.

This fully-resourced lesson describes the effects of enzyme and substrate concentration on the rate of enzyme-catalysed reactions. The PowerPoint and accompanying resources are the third in a series of 4 lessons which cover the details of point 3.2 (a) of the CIE A-level Biology specification. The first part of the lesson describes how an increase in substrate concentration will affect the rate of reaction when a fixed concentration of enzyme is used. Time is taken to introduce limiting factors and students will be challenged to identify substrate concentration as the limiting factor before the maximum rate is attained and then they are given discussion time to identify the possible factors after this point. A series of exam-style questions are used throughout the lesson and the mark schemes are displayed to allow the students to assess their understanding and for any misconceptions to be immediately addressed. Moving forwards, the students have to use their knowledge of substrate concentration to construct a graph to represent the relationship between enzyme concentration and rate of reaction and they have to explain the different sections of the graph and identify the limiting factors. The final section of the lesson describes how the availability of enzymes is controlled in living organisms. Students will come to recognise that this availability is the result of enzyme synthesis and enzyme degradation and a series of tasks will introduce the details of transcription and translation and therefore prepare them for the lessons in topic 6. Please note that this lesson explains the Biology behind the effect of concentration on enzyme-catalysed reactions and not the methodology involved in carrying out such an investigation as this is covered in a core practical lesson.

This lesson explains the effects of temperature increases on enzyme activity and describes how to calculate the temperature coefficient. The PowerPoint and the accompanying resource are part of the second lesson in a series of 3, which cover the content detailed in point 2.1.4 (d) [i] of the OCR A-level Biology A specification and this lesson has been specifically planned to tie in with an earlier lesson covering 2.1.4 (a, b & c) where the roles and mechanism of action of enzymes were introduced. The lesson begins by challenging the students to recognise optimum as a key term from its 6 synonyms that are shown on the board. Time is taken to ensure that the students understand that the optimum temperature is the temperature at which the most enzyme-product complexes are produced per second and therefore the temperature at which the rate of an enzyme-controlled reaction works at its maximum. The optimum temperatures of DNA polymerase in humans and in a thermophilic bacteria and RUBISCO in a tomato plant are used to demonstrate how different enzymes have different optimum temperatures and the roles of the latter two in the PCR and photosynthesis are briefly described to prepare students for these lessons in modules 6 and 5. Moving forwards, the next part of the lesson focuses on enzyme activity at temperatures below the optimum and at temperatures above the optimum. Students will understand that increasing the temperature increases the kinetic energy of the enzyme and substrate molecules, and this increases the likelihood of successful collisions and the production of enzyme-substrate and enzyme-product complexes. When considering the effect of increasing the temperature above the optimum, continual references are made to the previous lesson and the control of the shape of the active site by the tertiary structure. Students will be able to describe how the hydrogen and ionic bonds in the tertiary structure are broken by the vibrations associated with higher temperatures and are challenged to complete the graph to show how the rate of reaction decreases to 0 when the enzyme has denatured. The final part of the lesson introduces the Q10 temperature coefficient and students are challenged to apply this formula to calculate the value for a chemical reaction and a metabolic reaction to determine that enzyme-catalysed reactions have higher rates of reaction Please note that this lesson has been designed specifically to explain the relationship between the change in temperature and the rate of enzyme activity in a reaction and not the practical skills that is part of a lesson covering specification point 2.1.4 (d) [ii]

This lesson describes how to use and manipulate the magnification formula to calculate the magnification or the actual size in a range of units. The PowerPoint and accompanying resources have been designed to cover point 2.1.1 (e) of the OCR A-level Biology A specification and contains a number of quiz rounds as part of the competition that runs throughout all of the module 2.1.1 lessons The students are likely to have met the magnification formula at GCSE so this lesson has been written to build on that knowledge and to support them with more difficult questions when they have to calculate actual size without directly being given the magnification. A step by step guide is used to walk the students through the methodology and useful tips are provided. Students could be asked to calculate the actual size in millimetres, micrometres, nanometres or picometres so time is taken to ensure that they can convert between one and another.

This engaging lesson explains why coenzymes, cofactors and prosthetic groups are needed in some enzyme-controlled reactions. The PowerPoint and accompanying resource have been primarily designed to cover point 2.1.4 (e) of the OCR A-level Biology specification but can also be used as a revision lesson for the roles of ions as was covered back in module 2.1.2. The lesson begins with an introduction of the description of a cofactor and students will learn that some are permanently bound to the enzyme whilst others only form temporary associations. A quick quiz competition runs over the course of the lesson and is used to introduce prosthetic groups, mineral ion cofactors and organic coenzymes and zinc ions with carbonic anhydrase, chloride ions with amylase and NAD are used as examples of each type. The lesson has been planned to make links to related topics such as cations, anions, transport of carbon dioxide and respiration which will test students on their prior knowledge as well as prepare them for these topics in modules 3 and 5.

This lesson describes the light-dependent reactions of photosynthesis, focusing on the link to the light-independent reactions. The detailed PowerPoint and accompanying resources have been designed to cover the details included in point 5.7 of the Edexcel A-level Biology specification and therefore describes how light energy is trapped by exciting electrons in chlorophyll and the role of these electrons in generating ATP, reducing NADP in photophosphorylation and producing oxygen through photolysis of water. This is a topic which students tend to find difficult so this lesson has been intricately planned to walk them through each of the key reactions in the light-dependent stage. Time is taken to describe the roles of the major protein complexes that are embedded in the thylakoid membrane and this includes the two photosystems, the proton pump and ATP synthase. A series of exam-style questions have been written that link to other biological topics in this course such as cell structure and membrane transport as well as application questions to challenge them to apply their understanding. Some of these resources have been differentiated to allow students of differing abilities to access the work and to be pushed at the same time. Students will learn that there are two pathways that the electron can take from PSI and at the completion of the two tasks which describe each of these pathways, they will understand how ATP is generated in non-cyclic and cyclic fashion. The final task of the lesson asks them to compare these two forms of photophosphorylation to check that they understand when photolysis is involved and reduced NADP is formed. Due to the detail included in this lesson, it is estimated that it will take in excess of 2.5 hours of allocated A-level teaching time to complete

This lesson describes how the products of the light-independent reactions of photosynthesis are used by plants, animals and other organisms. The engaging and detailed PowerPoint and accompanying resources have been primarily designed to cover point 5.8 (ii) of the Pearson Edexcel A-level Biology A (Salters Nuffield) specification concerning the uses of GP and GALP but as the lesson makes continual references to biological molecules, it can act as a revision tool for a lot of the content of topic 1 and 2. The previous lesson described the light-independent reactions and this lesson builds on that understanding to demonstrate how the intermediates of the cycle, GP and GALP, are used. The start of the lesson challenges the students to identify two errors in a diagram of the cycle so that they can recall that most of the GALP molecules are used in the regeneration of ribulose bisphosphate. A quiz version of Pointless runs throughout the lesson and this is used to challenge the students to recall a biological molecule from its description. Once each molecule has been revealed, time is taken to go through the details of the formation and synthesis of this molecule from GALP or from GP in the case of fatty and amino acids. The following molecules are considered in detail during this lesson: glucose (and fructose and galactose) sucrose starch and cellulose glycerol and fatty acids amino acids nucleic acids A range of activities are used to challenge their prior knowledge of these molecules and mark schemes are always displayed for the exam-style questions to allow the students to assess their understanding. As detailed above, this lesson has been specifically written to tie in with the earlier lessons in this topic on the structure of the chloroplast and the light-dependent and light-independent reactions of photosynthesis

This fully-resourced lesson describes how Mycobacterium tuberculosis and Human Immunodeficiency virus infect human cells. The PowerPoint and accompanying resources have been designed to cover point 6.6 of the Pearson Edexcel A-level Biology A (Salters Nuffield) specification and ties in directly with the previous lesson where the structure of bacteria and viruses were compared. The lesson begins by ensuring that students recognise that TB is caused by the infection of a species of bacteria known as Mycobacterium tuberculosis and they will challenged to use their knowledge of scientific classification to recall that this pathogen is found in the mycobacteria genus. At this point, the students are told that the cell walls of this genus contain mycolic acids and later in the lesson they will have to work out that this specialist feature enables this pathogen to survive phagocytosis. A series of exam-style questions will challenge their knowledge of the respiratory and immune systems as they can understand how the bacterium travels to the alveoli where it is engulfed by a macrophage. Key terms like granuloma and necrosis are introduced and the sequence of events that occur following the formation of this aggregate of cells is described. The structure of viruses was covered during the previous lesson, so this next part of the lesson starts by challenging the students to recall the capsid, genetic material in the form of viral RNA and the lipid envelope. At this point, the students are introduced to gp120, the glycoprotein which is exposed on the surface of the lipid envelope, as this structure is critical for the entry of the virus into host cells. Students will annotate a basic diagram of HIV with these four structures which also has gp41 labelled. A quick quiz competition introduces the names of the enzymes found inside the capsid Moving forwards, the main task of this part of the lesson describes how HIV binds to the helper T cells, injects its capsid and integrates its DNA into the host’s genome in order to replicate to form virus particles (virions). Students are guided through the formation of a detailed answer about the mechanism of HIV and have to input key terms and structures where information is missing. Students will learn that the increase in the number of virus particles and a decrease in helper T cells and other immune cells results in infections like TB and by opportunistic pathogens and that this stage is recognised as AIDS