AS & A Level biology 2022 October/November.0610.11_ 1. student was provided with two test-tubes, one conti containing 10 cm? of solution Q. When these solutions hours, the concentration of P decreased but the concen The student wrote the following conclusions. 1 P may break down over time. (/ 2.Qmay be a biological catalyst. ad a 3 P may be the substrate for Q. Which conclusions could be supported by the information? — 2and 3 B1 and 2 only C1 only 2. Which statements are correct for the lock and key hypothesi enzyme action? ) 1 The substrate is the same shape as the active site. _/ 3 The enzyme and sometimes the substrate change shape sligh | re. enters the enzyme. KR and 2Ir increasing substrate Concentration ne rate of enzyme activity wit 3, Astudent investigated the F2t 7 epeated with the addition of @ reversible non-competitive enzyme ihr experiment was re graph was platted to show the results Which graph represents the results of the 1wo experiments o ‘enzyme enzyme actly sctiity ‘substrate substrate concentration concentration key — = without enzyme = inhibitor : . -==-= wih enzyme Inhibitor rate of rate of enzyme enzyme activity activity substrate ‘substrate concentration concentration AS & A Level biology 2022 October/November 0610 12 4. Which property of the tertiary structure of a globular protein enables it to catalyse metabolic reaction? {A Ithas hydrophobic amino acid R groups on the outside Ce will be denatured by high temperatures C The R groups of some amino acids form bonds with a substrate. (= three-dimensional shape depends on hydrogen bonding.tudent investic aN oA gated the effect of substrate concentration on the activity of The graph shows the results of this investigation, activity of enzyme ‘Substrate concentration An increase in which factors could lead to a change in the activity of the the graph? " 1 pH / 2 substrate concentration J 3 temperature dh (s)zams Biand2only Ctand3only D2and3only 6. The Michaelis-Menten constant, Km, is the substrate concentration at which an en at half its maximum rate. What is correct when the Km value is low? to its maximum rate. B_ The enzyme has a low affinity for the substrate and the slower its maximum rate. om 6) The enzyme has a high affinity for the “4 to its maximum rate.er7Noverber_0610.13 ology, 2022, 0¢t0b4 light. Changes in the structure’ oy As & A Level I AY 7, ) some molecules fuoresce when illuminat eZ shape of such molecules can chan 1ed with ultraviolet ne fluorescence: fa phosphate gfOUP .ge the intensity of # ish-green because ynthase fluoresces Plu .e catalyses the reactio The enzyme tryptophan 5 yn shown. active site. The enzym associated with the serine + indole — tryptophan but when indole is creases the intensity of the fluorescence, ‘Adding serine to the enzyme int ren fluorescence decreases in intensity: also added the bluish-gi sncluded from these observations? What may be co! 1 Serine and indole attach to the active site of the enzyme 2.An enzyme-serine complex is formed. 3 An enzyme-serine-indole complex is formed. A1,2and3 Bland2only C 1and 3 only D2and 3 onlycatalase 2H20, ““"“ 2H,0 + O2 The data is shown in the table, time/s malo Pe 30 157 60 254 : %0 233 - 420 285 | What explains the pattern of the data? ‘A The rate of reaction increases as more en: B The rate of reactio of oxygen released decreases as the enzymes begit C The volume 1 Jhe volume of onygen released decreases as more substrateis converte | 9. The Michaelis-Menten constant, Km, is a measure of the affinity of an enzym 4 The higher the affinity, the lower the Ko. 2 The lower the affinity, the slower the reaction will be. ds 3 At Ko half the active sites of the enzyme are 0 eo sly Which statements about Km are correct? A1,2and3AS & A Level biology 2022 May/June 0610 11 ’ 10. A student used colorimetry to monitor the hydrolysis of a protein by a protease enzyme,” The student used biuret solution to determine the concentration of protein in the hydrolysis reaction, The student produced a calibration curve using known concentrations of protein. Which diagram shows the calibration curve? A transmission absorbance o 0 Cee 0 protein concentration c transmission 0. 0 protein concentration _student completed an experim how increasing concentrati y al iment to measure how increasit creasing, " affects the rate of an enzyme-ci controlled react ion. competitive inhibitor, Which row deseri lescrib es the effect of a reversible competitive inhibitor on enzyme activity attachment of inhibitor] effect of increasing substrate concentration at active site ‘on rate of enzyme-controlled reaction ¢) oe) little effect on the rate aes, rate increases po} rate increases oD yes litle effect on the rate AS & A Level biology 2022 May/June 0610.12 low affinity for its substrate? has a high kn and reaches Vis at a high substrate concentration, B it has a high ke and reaches Vnw« at a low substrate concentration. CIthas a low Km and reaches Vina at a high substrate concentration. +5 Which statements describe similarities betwe 1 They are both globular proteins. i Atand2 (hres C1only14. What is a feature of competitive enzyme inhibition? ently to the active site. 7 L@pniviion can be reversed by increasing the concentration of the substrate ndary structure of the enzyme. >< A The inhibitor binds perman The inhibitor molecule changes the secor D The substrate and the inhibitor are the same shape. V AS&A Level biology 2022, February/March 0610.12 415, Which relationships could be investigated using a colorimeter? the effect of light intensity on the rate at which a soluti from green to colourless 2 the effect of temperature on the rate of breakdown. of cell membranes | pigmented cells, such as beetroot (red beet)” ate of release of oxygen from the 3 the effect of pH on the re . by catalase x Athe effect of light intensity on the rate cof change of skin colour | in bright light x 1,2, 3.and4 and 2 only anne Hae 2 ~