Monday, 10/3Topic 7 TEST WEDNESDAY!

Explain the secondary and tertiary levels of protein structure. 4 marks

secondary structure: [2 max]folding / pleating of polypeptides to form b - pleated sheets / coiling of polypeptides to form a -helix;held in place by hydrogen bonds;make structure stable;contributes to strength of fibrous proteins;provide structural role in organisms;eg a -helix is keratin / b-sheet is silk;

tertiary structure: [2 max]3-D shape;due to bonding between amino R-groups / residues;hydrogen bonds / disulphide bridges / sulphur bonds / ionic bonds;form globular proteins;which are soluble;eg lysozyme / enzymes;

7.6Enzymes

7.6.1 State that metabolic pathways consist of enzyme-catalysed reactions in:Chemical rxns usually multiple stepsEach step has own enzyme Chains (glycolysis)Cycles (Krebs, Calvin Cycles)

7.6.2 Describe the induced-fit model. (1958)Extension of lock-and-key model (1894)Accounts for ability of some enzymes to bind to several substrates w/similar rxnsActive site may not be as rigid as originally thoughtShape adapts somewhat perfect fitAllows slightly diff substrates to fit

Analogy: glove fits on several diff hands...but not on a foot

7.6.3 Explain that enzymes lower the activation energy of the chemical reactions that they catalyse.Speed up rxn, but dont change enzyme & dont get used upRxns require activation energyActive site facilitates changeLowers activation energyCollisions: higher act energy = need faster collision speed More molecules able to react, rate of rxn increasesExothermic Rxn

7.6.4 Explain the difference between competitive and non-competitive inhibition, with reference to one example of each.Competitive inhibition inhibiting molecule is structurally similar to substrate molecule ... COMPETES!binds to active site, prevents substrate bindingAdd more substrate, decrease effect of inhibitor

7.6.4 Explain the difference between competitive and non-competitive inhibition, with reference to one example of each.EX: Prontosil (antibacterial drug) inhibits synthesis of folic acid (vit B) in bacteria drug binds to enzyme that makes folic acid need folic acid for nucleic acid synthesis Prontosil bacterial cell dies b/c cant make DNA/RNA

Animal cells not affected b/c dont MAKE folic acid, get it from food. (no enzyme, so no effect)

7.6.4 Explain the difference between competitive and non-competitive inhibition, with reference to one example of each.Non-competitive inhibitioninhibitor binds to an enzyme (not to its active site) causes conformational change in active site decrease in activityAdding more substrate: no effect

7.6.4 Explain the difference between competitive and non-competitive inhibition, with reference to one example of each.Non-competitive inhibitionEx: CYANIDEattaches to SH groups in cytochrome c oxidase, destroys disulfide bridges, changes tertiary structure, no function(normally catalyzes reduction of oxygen to water, so without it cell respiration stops, organism dies)

7.6.5 Explain the control of metabolic pathways by end-product inhibition, including the role of allosteric sites.Allostery = type of non-compet. inhibitionallosteric site binding Reversible change in shape of ASAllosteric activators speed up rxnAllosteric inhibitors slow down rxnend product of pathway can be allosteric inhibitor

7.6.5 Explain the control of metabolic pathways by end-product inhibition, including the role of allosteric sites.Another example: Glycolysis[product] increases, fits in allosteric site of previous enzyme in pathway, changes active site, reduces/stops rxnsLevel of product reduced...enzyme releases allosteric molecule, active site changes back to normal, rxns proceed