[Answered] Contact Us for this Answer +1 323-412-5597 / support@studentscoursework.com Biochemistry examPlease answer all of the exam questions.Choose the best answer choice provided. Consider a di-glycine dipeptide (e.g. two glycine amino acids that have been covalently bonded together via a peptide bond). If the amino group is neutral and the C-terminal carboxy group is deprotonated which pH value do you expect is most consistent with these observations? Flag this QuestionQuestion 32.5 pts An arginine residue (Arg 210) in the a subunit of the E.coli ATP synthase is near the aspartate residue (Asp 61) in the matrix-side proton channel. How might Arg 210 assist proton flow? Flag this QuestionQuestion 42.5 pts Thiamine thiazolone pyrophosphate binds to pyruvate dehydrogenase about 20000 times as strongly as does thiamine pyrophosphate. Why? Flag this QuestionQuestion 52.5 pts The oxidation of malate by NAD+ to form oxaloacetate is a highly endergonic reaction under standard conditions with a ΔG∘ of 29 kJ mol-1. The reaction proceeds readily under physiological conditions. Assuming an [NAD+]/[NADH] ratio of 3 and pH 7 (25 degrees C) what is the lowest [malate]/[oxaloacetate] ratio at which oxaloacetate can be formed from malate? Flag this QuestionQuestion 62.5 pts Which of the following inhibits the pyruvate dehydrogenase complex? Flag this QuestionQuestion 72.5 pts During glycolysis what is the net number of ATP molecules produced from one molecule of glucose? Flag this QuestionQuestion 82.5 pts A residue in a folded protein has a phi torsion angle value of -80 degrees and a psi torsion angle value of 120 degrees. This residue will probably be part of: Flag this QuestionQuestion 92.5 pts The ΔG∘ for the reaction catalyzed by enolase is +1.7 kJ/mol while its ΔG under physiological conditions is -3.3 kJ/mol. Explain this difference. Flag this QuestionQuestion 102.5 pts What will be the consequence of inhibiting the pyruvate dehydrogenase-specific phosphatase regulatory enzyme? Flag this QuestionQuestion 112.5 pts What is the function of the γ-subunit of ATP synthase during oxidative phosphorylation? Flag this QuestionQuestion 122.5 pts A non-spontaneous reaction can be made to occur spontaneously (e.g. reactants are converted into product to achieve equilibrium) by: Flag this QuestionQuestion 132.5 pts Which constant of Michaelis-Menten kinetics is most likely to be an estimate of an enzymes affinity for its substrate? Flag this QuestionQuestion 142.5 pts Which of the following is true for enzyme-catalyzed reactions? Flag this QuestionQuestion 152.5 pts Which glucose transporters have the highest affinity for glucose in humans? Flag this QuestionQuestion 162.5 pts For an enzyme that follows simple Michaelis-Menten kinetics what is the value of VMAX if v0 is equal to 8.9 umol min-1 at a substrate concentration equal to twice the value of KM? Flag this QuestionQuestion 172.5 pts Predict which conditions would be most favorable for α-helix formation of a peptide containing poly-glutamic acid residues. Flag this QuestionQuestion 182.5 pts What are the thioesters in the reaction catalyzed by the pyruvate dehydrogenase complex? Flag this QuestionQuestion 192.5 pts Write a balanced equation for the conversion of glucose into pyruvate. Flag this QuestionQuestion 202.5 pts The Q-cycle: Flag this QuestionQuestion 212.5 pts This complex participates in both the Citric Acid Cycle as well as the electron transport chain during oxidative phosphorylation: Flag this QuestionQuestion 222.5 pts Why do isolated F1 subunits of ATP synthase catalyze ATP hydrolysis? Flag this QuestionQuestion 232.5 pts Which enzymes have regulatory roles in glycolysis? Flag this QuestionQuestion 242.5 pts How many oxidation-reduction reactions occur during glycolysis? Flag this QuestionQuestion 252.5 pts What is the purpose for the anaerobic fermentation of pyruvate? Flag this QuestionQuestion 262.5 pts GAP dehydrogenase forms a covalent thioester intermediate with the substrate. Why? Flag this QuestionQuestion 272.5 pts Glucose labeled with 14C at C5 is incubated with the glycolytic enzymes and necessary cofactors. What is the distribution of 14C in the pyruvate that is formed assuming that DHAP is rapidly converted to GAP? Flag this QuestionQuestion 282.5 pts Electron flow down the electron-transport chain leads to the: Flag this QuestionQuestion 292.5 pts You are studying a new bacterial organism Kleigeritis and discover that it has a strange Citric Acid Cycle. Specifically you find out that succinate dehydrogenase catalyzes the oxidization of succinate and the reduction of Coenzyme Q directly. What is the ΔG∘ for this mysterious reaction? Please use Table 18.1 for the standard reduction potentials and 96 kJ mol-1 V-1 for Faradays constant. Flag this QuestionQuestion 302.5 pts Fully oxidized carbons leave the citric acid cycle as: Flag this QuestionQuestion 312.5 pts All four carbon atoms of oxaloacetate are labeled with radioactive 14C. The labeled oxaloacetate is incubated with all of the enzymes substrates and cofactors necessary for the citric acid cycle (CAC). After one round of the CAC where do you expect to find the radioactive carbons? Flag this QuestionQuestion 322.5 pts The synthesis of citrate from acetyl CoA and oxaloacetate is a biosynthetic reaction. What is the energy source that drives formation of citrate? Flag this QuestionQuestion 332.5 pts What is the pH of a 1 M solution of an acid with a pKa of 3.5? Flag this QuestionQuestion 342.5 pts Carbon atoms from glucose enter the citric acid cycle in the form of: Flag this QuestionQuestion 352.5 pts HCO3 – is labeled with radioactive 14C and incubated with all the enzymes substrates and cofactors necessary for gluconeogenesis. Which atoms of glucose will be labeled with 14C? Flag this QuestionQuestion 362.5 pts What type of reaction is catalyzed by aconitase? Flag this QuestionQuestion 372.5 pts The folded state of proteins is primarily stabilized by: Flag this QuestionQuestion 382.5 pts Enzymes are powerful because they often create microenvironents where the pKavalues of important ionizable groups and both the substrate and the enzyme can be manipulated to achieve catalysis. Which answer is most consistent with an environment that will shift the pKa of a lysine side-chain amino group down (e.g. lower than normal)? Flag this QuestionQuestion 392.5 pts How many high-energy phosphate bonds are expended in gluconeogenesis to generate one molecule of glucose starting from 2 pyruvate? Flag this QuestionQuestion 402.5 pts Which of the following is true under the following conditions: The enzyme concentration is 500 nM the substrate concentration is 5 mM and the KM is 5 micromolar.

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