(a)
To show: At equilibrium,
Introduction: Free energy of a system is that amount of energy that can be changed into work in a system provided that the temperature and pressure of the system remain the same. It is denoted by
(b)
To determine: The amount of work that can be done by the system.
Introduction: Free energy of a system is that amount of energy that can be changed into work in a system provided that the temperature and pressure of the system remain the same. It is denoted by
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Becker's World of the Cell (9th Edition)
- For 100 words. What are the two essential requirements to effectively carry out metabolic work?arrow_forwardX Incorrect. Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the reaction? Choose all that are correct. The enzyme increases the AG value. The enzyme increases the rate of reaction. The enzyme decreases the rate of reaction. The enzyme decreases the AG value. The enzyme raises the activation energy. The enzyme lowers the activation energy.arrow_forwardChemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition prevents it from cleaving nearby covalent bonds. HCI + CH, C-O Chymotrypsin-His 57 TPCK Modified enzyme True O Falsearrow_forward
- More ratios. Through the use of nuclear magnetic resonance spectroscopy, it is possible to determine the ratio between the protonated and deprotonated forms of buffers. (a) Suppose the ratio of [ A- ]A I to [HA] is determined to be 0.1 for a buffer with pKar6.0.pKa = 6.0. What is the pH? (b) For a different buffer, 91974 suppose the ratio of [ A- ]lA J to [HA] is determined to be 0.1 and the pHpH is 7.0. In this case, what is the pKapKa of the buffer? (c) For another buffer with pKa=7.5PKa = 7.5 at pH 8.0pH 8.0, what is the expected ratio of [ A- ][A ] to [HA]? doarrow_forwardHelp please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!arrow_forwardBalance the reactions. A hint is provided to help you decide if the reaction will proceed as written, ie from left to right. Do not leave any fractions. 1. a) Balance Al₂O3 → Al + 0₂ b) What type of reaction is this? c) Is this a redox rx, yes / no ? d) The reaction will go from left to right, yes / no ? (hint: O₂ is very reactive) 2. a) Balance HNO3 + AI → b) What type of reaction is this? c) Is this a redox rx, yes / no ? d) The reaction will go from left to right, yes / no ? (hint: aluminum is a reactive metal, and a gas escapes) C7H14 + 0₂ 3. a) Balance, leave no fractions b) What type of reaction is this? c) Is this a redox rx, yes / no ? d) The reaction will go from left to right, yes / no ? (hint: O₂ is very reactive) H2(g) + AI(NO3)3 → CO₂ + H₂Oarrow_forward
- Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?arrow_forwardOn the trail of carbons. Tissue culture cells were incubated with glutamine labeled with 15NN in the amide group. Subsequently, IMP was isolated and found to contain some 15N.N. Which atoms in IMP were labeled?arrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forward
- Thank you in advance!Based on the model on the picture, please help me identify these (even with no explanation):1. What is free energy? What is its symbol? 2. For an exergonic reaction, what is the value of △G? 3. For an endergonic, what is the value of △G? 4 What are the factors that affect △G? 5. What is energy coupling? In a coupling reaction, what must be the overall value of △G? 6. What does the cell do with the energy produced from exergonic reactions? 7. What molecule does the cell use as an energy carrier? Draw its structure. 8. Why is it that this energy carrier is considered to be high energy containing phosphate? 9. Bond of this energy carrier of cells is broken through what?arrow_forwardENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forwardO BIOCHEMISTRY Understanding major biochemical energy storage and release. A certain anabolic biochemical reaction A has AG- 17.8 kJ mol , and is always coupled to another reaction B, which has two reactants and two products, I this: R + R2 P + P2 The molecule in the drawing area below is either R, or P. • If it's R, change it into P. But if it's P, change it into R. • In either case, draw the molecule as it would exist at physiological pH. • Also please answer the questions about Reaction B in the table below. OR, Was the molecule in the drawing area R, or P, before you changed it? What is R? Enter its common name, usual symbol, or chemical formula: What is P2? Enter its common name, usual symbol, or chemical formula: O BIOCHEMISTRY Understanding major biochemical energy storage and release.. ODO its common name, usual symbol, or chemical formula: NH, -CH N. H OH OH ...... to IIIarrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning