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Cell biology
Biological molecules
Organisation
Infection and response
Energy transfers (a2 only)
Homeostasis and response
Responding to change (a2 only)
The control of gene expression (a-level only)
Substance exchange
Bioenergetics
Genetic information & variation
Inheritance, variation and evolution
Genetics & ecosystems (a2 only)
Ecology
Cells
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1c the tudors: england, 1485-1603
1l the quest for political stability: germany, 1871-1991
Inter-war germany
1f industrialisation and the people: britain, c1783-1885
Britain & the wider world: 1745 -1901
2n revolution and dictatorship: russia, 1917-1953
2j america: a nation divided, c1845-1877
The cold war
World war two & the holocaust
World war one
Medieval period: 1066 -1509
The fight for female suffrage
2m wars and welfare: britain in transition, 1906-1957
2d religious conflict and the church in england, c1529-c1570
Britain: 1509 -1745
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15/10/2022
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• Enzymes are biological catalysts • Made of globular proteins • Highly specific shape maintained by chemical bonds (hydrogen, ionic, disulphide bridges) • They have an active site into which fits the substrate to form the enzyme-substrate complex. • Releases products immediately so that they active side is free again allowing the enzyme to be reused. • Involved en anabolic (building) and catabolic (breaking) reactions. • Enzymes can be found intercellularly and extracellularly The active site is only formed by a small number of the amino acids in the polypeptide chains but the shape of the enzyme is determined by the sequence of amino acids in the entire chain the primary structure and the bonds that form at the secondary and tertiary structure stage Catalysts affect the rate of chemical reaction without undergoing permanent change and therefore is effective in small amounts. Collision theory • Molecules have kinetic energy and more around randomly. • For two molecules react they must first collide with enough energy to overcome the activation energy barrier and react. • Not all collisions have enough energy and lead to a reaction • Enzymes work by lowering the activation energy. Induced fit model of enzyme action • Enzymes actually change shape slightly to fit the profile of the substrate. • Enzyme has a general shape but is flexible...
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and can mould itself around the substrate •The active site forms as the enzyme and substrate interact. • Before the reaction, the active site is not complementary • Shape of the active site changes slightly as substrate binds and the enzyme/substrate complex is formed • As it changes shape, the enzyme puts a strain on the substrate molecule, distorting the bonds and lowering the activation energy. Enzyme Action Reactants: Glucose +0, Enzymes Without enzyme With enzyme Activation energy without enzyme Activation energy with enzyme Overall energy released during reaction Products: CÓ, + HỌ a) Lock and key b) Induced fit c) Conformational selection They allow reactions to happen at a lower temperature than they would without the enzyme being present. This is because they either hold substrates close together reducing repulsion and allowing them to bond more easily or put more strain on the bonds of a substrate allowing them to break apart more easily Denaturing means that the hydrogen bonds begin to break and the tertiary structure begins to unfold meaning the enzyme can no longer function as its active site is no longer complimentary to the substrate Rate of reaction Rate of reaction (H) 1 Temperature Optimum pH pH 3 PHI-logio Lut Rate of reaction Rate of reaction Enzyme concentration limiting factor Enzyme concentration Substrate concentration limiting factor Enzyme concentration limiting factor Substrate concentration Inhibitors Inhibitors reduce enzyme activity. Some bind permanently but many just make temporary attachments to the enzymes active site. There are two types of reversible inhibitors. Competitive • Have a similar shape to the substrate • Can empty active site. • Compete with substrate for the active site so the amount of inhibition depends on the relative concentrations of substrate and inhibitor Non-competitive • Attach themselves to the enzymes away from the active site. • They alter the shape of the active site. • As they are not in competition, adding more substrate will not decrease the effect of the inhibitor • An enzyme is a biological catalyst made of globular proteins with the purpose of lowering activation energy without running out • The enzyme binds with the substrate via its complimentary active site to form a enzyme substrate complex