cell biology exam 2 study guide
cell biology exam 2 study guide BSC322
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This 16 page Study Guide was uploaded by Sarah Ferrier on Saturday October 10, 2015. The Study Guide belongs to BSC322 at Marshall University taught by Dr. Harrison in Fall 2015. Since its upload, it has received 381 views. For similar materials see Cell Biology in Biology at Marshall University.
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Date Created: 10/10/15
Exam 2 O9 3 Need to know gt Enzyme basic structure Substrate function ase Substrate ase used for hydrolytic enzymes Globular protein and cofactor Primary secondary tertiary quaternary gt Km Vmax competitive vs noncompetitive inhibition When S becomes very large the value of V reaches a maximum 0 Can be increased by adding more enzyme 0 Determined by time required for catalytic reaction and how many enzyme molecules are present Km is MichaelisMenten constant 0 Concentration of substrate that gives half Vmax Competitive inhibitors bind active site of enzyme and compete With substrate for active site 0 Prevents substrate from binding 0 Same VmaX as uninhibited reaction but Km has changed Noncompetitive inhibitors bind enzyme molecule outside of the active site 0 Same Km was uninhibited reactions but VmaX has changed 0 Causes a conformation change gt Enzyme nomenclature and classification Substrate function ase Substrate ase used for hydrolytic enzymes Oxidoreductases transferases hydrolases lyases isomerases ligases gt LineweaverBurk equations Doublereciprocal Q1 This is a MichaelisMenten graph for glucose uptake into red blood cells from a normal individual Determine the VmaX value for this graph v umol39min BUD 39 500 400 39 300 39 200 100 Connol 53 2 5 10 15 2D Glucose mM A1 500 umolminl Q2 This is a MichaelisMenten graph for glucose uptake into red blood cells from a normal individual Determine the Km value for this graph BUD 39 SUD Control 400 soo 3 2oo gt 100 U A n U 5 10 15 2D Glucose mM A2 2 mM Q3 This is a MichaelisMenten graph for glucose uptake into red blood cells from a normal indiVidual Which reaction component is limiting during the part of the curve labeled 2 800 V Control 01 D D h D O 2 v lllllle lllill M 00 D O D D A D D 1 O o 5 1o 15 2o Glucose mM A3 Number of enzymes present Q4 This is a MichaelisMenten graph for glucose uptake into red blood cells from a patient With type2 diabetes compared to a normal patient Control Which parameter is different between these indiViduals 600 500 Control A E 400 5 300 g Patient v zoo gt 100 l 0 o 5 1o 15 20 Glucose mM A4 Km Q5 Determine the Km value for this graph 30 N I39J39I I 03 Cl I If minim l E A5 50 um Q6 The Vmax of the inhibited reaction is 100 inhibito 9 0 L nounal v39v milrumol g 0005 0000 0005 0010 0015 0020 0025 1 gaactose InM 391 l A6 05 umol min1 Q7 What would be the effect of this substitution from A T at amino acid 188 in terms of changes in the enzymes structure A7 Conformation of the enzyme could be altered around site 188 Q8 W in terms of function A8 Enzyme would be altered in its active site Q9 Consider an enzyme that is active in the uncomplexed form Which has high affinity for its substrate Therefore binding of an allosteric inhibitor stabilizes the enzyme in its low affinity form A9 True Q10 A plot of enzyme velocity against temperature for an enzyme indicates little activity at 0 C and 40 C with peak activity at 35 C The most reasonable explanation for the low velocity at 0 C is that at this temperature A10 there is too little activation energy available from the environment Q11 Which of the following is true of an enzyme An enzyme A11 Acts as a biological catalyst Q12 The Michaelis constant Km refers to the at which a reaction proceeds at of the maximum velocity The Km most accurately re ects A12 substrate concentration 12 the affinity of the substrate enzyme interaction Q13 binds to an enzyme covalently causing a loss of catalytic activity A13 An irreversible inhibitor Q14 The phosphorylation of glucose to generate glucose 6 phosphate is catalyzed by the enzyme hexokinase This enzyme however is allosterically inhibited by its own product glucose 6 phosphate This is an example of A14 feedback regulation Q15 Enzymes that catalyze the phosphorylation of other enzymes are A15 Protein kinases 339 Need to know gt Basic structure of phospholipids I 2 fatty acids and phosphate group I Small hydrophilic alcohol head I Amphipathic nature gt Basic structure of membrane proteins I Integral membrane proteins 0 Hydrophobic regions embedded within membrane interior 0 Hydrophilic regions that extend outward I Peripheral proteins 0 Bound to membrane surfaces through weak electrostatic forces and hydrogen bonding I Lipidanchored proteins 0 Polypeptide chains are located on one on the surfaces of the lipid bilayer but are covalently bound to lipid molecules embedded within the bilayer Q1 Fatty acids are highly reduced and so yield a large amount of energy upon oxidation A1 True Q2 Which of the following is not a type of lipid A2 Glycogen Q3 Which of the following fatty acids is saturated Nlumiber Number of Common of Carbons Double Bonds Marries 1 8 Cl Stearate 16 1 Palmitoleate 18 1 O lea39te 13 Linoleate A3 Stearate Q4 This model shows which of the following membrane components A4 Phospholipids glycolipids proteins sterols Q5 With respect to the outer and inner faces of the lipid bilayer of the cell membrane the composition of proteins is A5 Asymmetrical Q6 Cholesterol is Q6 A sterol Q7 Localized regions of membrane lipids that contain proteins involved in cell signaling are known as A7 Lipid rafts Q8 The hydrolytic enzyme that breaks sucrose into glucose and fructose A8 Sucrase Q9 Lipids differ from other large biological molecules in that they A9 Are not true polymers Q10 The characteristic that all lipids have in common is that A10 none of them has significant solubility in water Q11 Estradiol cortisol and aldosterone are all A11 steroid hormones Q12 fatty acids have and contribute to increased membrane uidity A12 unsaturated double bonds Q13 A cellular biologist eXposes both sides of a membrane to a uorescent chemical that non specifically labels proteins eXposed to the aqueous solvent but not portions of those proteins eXposed to the interior of the membrane enVironment Which of the following classes of proteins would not be labeled on both sides of the membrane A13 Integral monotopic Embedded on only one side does not span entire membrane Q14 Ankyrin is a peripheral membrane protein found in erythrocytes Therefore it A14 lacks discrete hydrophobic sequences Q15 You discover an integral membrane protein that has terminal sialic acid groups attached to amino acid residues Via N and O links It is therefore most likely A15 A glycoprotein Q16 Assume that you and your lab partner have made the following artificial membranes Membrane 1 made entirely of phosphatidylcholine with saturated 16 carbon fatty acids Membrane 2 same as membrane 1 except that each of the 16 carbon fatty acids has a single as double bond Membrane 3 same as membrane 1 except that each of the saturated fatty acids has only 14 carbons The three temperatures you determine are 36 C 23 C and 41 C Assign each of these transition temperatures to the correct artificial membrane and eXplain your reasoning Membrane 1 41 C Membrane 2 23 C Membrane 3 36 C 339 Need to know gt Hypertonic hypotonic and isotonic solutions HYPERTONIC ISOTONIC HYPOTONIC SOLUTION SOLUTION SOLUTION H20 H20 H20 ANIMAL lt CELL a Shriveled Normal Flaccid Turgid Plasmolyzed gt Facilitated and active transport examples ATPase pumps NaK pumps Erythrocyte plasma membrane gt Types of gated channels Voltage Ligand Mechanosensitive gt Types of transport ATPases Ptype o Reversibly phosphorylated by ATP 0 810 transmembrane segments 0 Ion gradients 0 Protein pumping 0 Plasma membrane Vtype 0 vacuoles organelles 0 Protein pumping F type o Bacteria mitochondria chloroplasts 0 Big motor 0 Gradients can be used as energy source to synthesize ATP 0 ATP synthases o Proton channel ABCtype o transporters 0 Embedded in membrane 0 Peripheral proteins 0 4 polypeptides 0 Resistance to drugs Q1 A red blood cell is normally in a situation A1 Isotonic Q2 A red blood cell shrinks when it is put into a salt solution Therefore the red blood cell moved from a to a situation A2 Isotonic hypertonic Q3 When transport proteins move solutes against the concentration gradient this is called A3 Active transport Q4 When solutes move to regions of lower concentration with the aid of transport proteins this is called A4 Facilitated diffusion Q5 In the lea ets in a sensitive plant Mimosa potassium ions are pumped out of specialized motor cells most likely by A5 Active transport Q6 The lea ets in a sensitive plant Mimosa accumulation of potassium outside of the motor cells causes A6 water to move out of the motor cells causing them to collapse Q7 From the bioinformatics information the glucose transporter GLUTl has 12 hydrophobic d helixes and therefore is an membrane protein A7 Multipass integral Q8 From the bioinformatics information the glucose transporter GLUTl has 12 hydrophobic d helixes and therefore is an membrane protein A8 Hexokinase Q9 Glucose uptake into intestinal cells by a Na glucose symporter In this system the inward transport of glucose against its concentration gradient is driven by the simultaneous inward transport of Na ions down their electrochemical gradient Therefore the Na glucose symporter is considered A9 Indirect active transport Q10 Indicate the property which can be used to distinguish between each of the following pairs of transport mechanisms a Facilitated diffusion active transport 1 Requirement for metabolic energy b Simple diffusion active transport 1 Direction the solute moves relative to its concentration gradient or its electrochemical potential 0 Symport antiport 1 Intrinsic directionality d Uniport coupled transport 1 Requirement for simultaneous transport of two solutes Q11 Answer with D if the statement is true of simple diffusion F if its facilitated diffusion A if active transport N for none Requires the presence of an integral membrane protein F Depends primarily on solubility properties of the solute N osmosis Involves proteins called ATPases A Applies only to small nonpolar solutes D A Michaelis constant Km can be calculated F Q12 Which of the following statements is true comparing the simple diffusion of a substance across a membrane vs the facilitatedactive movement of a substance across a membrane A12 Simple diffusion differs from facilitated diffusion and active transport in that it is not dependent on a membrane protein does not exhibit saturation kinetics and is not subject to competitive inhibition Q13 The rate of simple diffusion of a polar molecule across a membrane is directly and linearly proportional to The thickness of a membrane is eXpected to be to the rate of simple diffusion for polar molecules A13 its concentration difference across the membrane inversely proportional Q14 Active transport is the protein mediated movement of substances A14 Against a concentration gradient Q15 This type of ATPase carries the widest variety of solutes A15 ABC type Q16 in comparing symports to antiports it can be said that A16 they can be ATP driven pumps 339 Need to know gt Inputoutput initial substrates and products 39 Start With 2 ATP end With 4 ATP net 2 ATP I End With 2 NADH 2 H20 2 H and 2 pyruvates Q1 In the overall reaction for the complete breakdown glucose C6H1206 602 9 6H20 and 6C02 The oxygen from glucose becomes part of Al H20 Q2 Enzyme Which catalyzes this reaction Fructose 6 Fructose16 phosphate bisphosphate A1 Phosphofructokinase Q3 Enzyme Which catalyzes this reaction 0 if C H C H 39 4 39 H C OH m H C OH HO C H HO C H H C OH H C OH W I H C OH H C OH H C OH H C O H H Glucose6 phosphate A3 Hexokinase Q4 Which glycolytic enzyme uses ATP as a substrate A4 Phosphofructokinase Q5 For both prokarytoic and eukaryotic cells the enzymes for glycolysis are found in the cytosol A5 True Q6 Enzyme which catalyzes this reaction 0 II c o gt i0 CH3 c w i C H I CH3 A6 Pyruvate decarboxylase Q7 Enzyme E8 1mm mm was Galactosed phosphate II 7Ht 39 ie UDPgalactose lt59 o 9quot A7 Lactase E11 Q8 High ATP stimulates A8 Gluconeogenesis Q9 High F26BP stimulates A9 Glycolysis Q10 Michaelis Menten plot of liver phosphofructokinase PFKl activity demonstrates that fructose26bisphosphate is 100 gt5 59 01 3 mM 5 fructose 26 g bisphosphate g 50 C 9 No fructose26 72 bisphosphate 39E Fructose6phosphate A10 an allosteric activator of PFKl Q11 In the allosteric inhibition of liver phosphofructokinase PFKl by ATP high ATP causes the Km to thus the affinity of the enzyme for its substrate 100 gt5 Low ATP 3 g 50 5 3 3 High ATP Fructose 6 phosphate A11 Increase decreasing Q12 Which of the following accurately summarizes the substrate level phosphorylation strategy of ATP synthesis in glycolysis A12 Phosphate groups are transferred exergonically from high energy phosphorylated intermediates to ADP to make ATP Q13 Anabolic pathways A13 involve biosynthesis Q14 The glycolytic enzymes that are allosterically regulated are A14 enzymes that catalyze reactions with large negative delta G39s Q15 In comparing glycolysis and gluconeogenesis it can be said that A15 only gluconeogenesis has a 4 carbon intermediate 339 Need to know gt Mitochondria Krebs cycle and electron transport chain input output initial substrates and products I Start with 2 pyruvates NAD ADP and Phosphate group end with NADH C02 ATP FADH2 I The TCA cycle accomplishes the following 0 1 Two carbons enter the cycle as acetyl CoA which joins oxaloacetate to form the six carbon citrate 0 2 Decarboxylation occurs at two steps to balance the input of two carbons by releasing two C02 0 3 Oxidation occurs at four steps with NAD the electron acceptor in three steps and FAD in one o 4 ATP is generated at one point with GTP as an intermediate in the case of animal cells 0 5 One turn of the cycle is completed as oxaloacetate the original 4C acceptor is regenerated I Aerobic respiration summing it up 0 As carbohydrates and fats are oxidized to generate energy coenzymes are reduced 0 These reduced coenzymes represent a storage form of the energy released during oxidation 0 This energy can be used to drive ATP synthesis as the enzymes are reoxidized by the ETS 0 As electrons are transported from NADH or FADH2 to 02 they pass through respiratory complexes where proton pumping is coupled to electron transport 0 The resulting electrochemical gradient serves as the driving force for ATP synthesis gt Identify of the locations and functions of the electron transport chains and ATPsynthases in mitochondria I Matrix I Pumping of protons Q1 Enzyme TCA6 o c o E v 2 00 039 A1 Succinate dehydrogenase Q2 In the Krebs cycle acetyl COA is degraded to A2 CO2 Q3 Uses acetyl CoA to produce ATP by substrate level phosphorylation A3 KrebsTCA cycle Q4 Produces pyruvate A4 Glycolysis GLUCOSE esp gt A V GIucoseGphosphate Fz sap 0 FructoseGphosphate F1GBP 6 ATP gt Acetyl CoA Acetyl CoA 25 Paavson Eautmpan In Q5 Gly l Gly 3 and Gly lO are allosteric enzymes True Q6 High ATP inhibits A6 Glycolysis Q7 A membrane vesicle preparation that is able to transport electrons and synthesize ATP When the vesicles are placed in a pH 4 buffer so they take up protons the membranes lack the ability to make ATP However when the pH 4 membrane vesicles are washed and immersed in a pH 8 buffer ATP synthesis activity occurs From these results you interpret that A7 a pH gradient is necessary for ATP synthesis where there needs to be are more protons inside the vesicle compared to outside Q8 You incubate isolated intact mitochondria in a buffered solution containing succinate an oxidizable substrate and ADP plus Pi Upon adding cyanide an inhibitor of Complex IV cyto chrome oxidase you examine the effect on oxygen consumption and the production of ATP What do you predict A8 Oxygen will not be consumed and no ATP will be produced
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