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Principles Of Pharmacology Med Assist

Principles Of Pharmacology Med Assist

6th Edition

ISBN:9781337512442

Author:RICE

Publisher:RICE

Chapter1: Numerals And Fractions

Section: Chapter Questions

Problem 7RP

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Question

Identify the equilibrium expression for the reaction:
2 NO(g) N2(g) + O2(g)
K-
[N][O]
2[NO]
O [NO]
K-
[N][O]
[N][O]
K=
[NO]
O [N,]+[0]
K-
[NO]
OK-[N][O][NO]
D

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Dehalogenase enzymes catalyze the clevage of C-X bonds. One such dehalogenase catalyzes the following reaction. An active site aspartate is thought to carry out the initial nucleophilic attack that expels the chloride. Select the most likely intermediate in the reaction. (Note the stereochemistry. Refer to P11.19 in the textbook if needed.) O O A C D OE -CH₂ H H₂C™ CO₂ H B CO₂ CI N H₂O Cr CO₂ H CO₂ нотум CH3 D CO₂ five N E CH₂
Balance each of the following redox reactions occurring in acidic solution. |-(aq)+NO-2(aq)→12(s)+NO(g)l-(aq)+NO2- (aq)→12(s)+NO(g) Express your answer as a chemical equation. Identify all of the phases in your answer. ClO-4(aq)+Cl-(aq)→CIO-3(aq)+CI2(g)CIO4- (aq)+Cl-(aq)→Cİ03-(aq)+Cl2(g) Express your answer as a chemical equation. Identify all of the phases in your answer. NO-3(aq)+Sn2+(aq)→Sn4+(aq)+NO(g)NO3- (aq)+Sn2+(aq)→Sn4+(aq)+NO(g) Express your answer as a chemical equation. Identify all of the phases in your answer.
Write a balanced equation for each of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Glc (d) The conversion of 2 moles of glycerol toglucose (e) The conversion of 2 moles of malate to glucose-6-phosphate
A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction The researchers begin to characterize the enzyme. (a) In the first experiment, with [Et] at 4 nM, they find that the Vmax is 1.6 uM/s. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) (b) In another experiment, with [Et] at 1 nM and [HAPPY] at 30 uM, the researchers find that V0 = 300 nM/s. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) (c) Further research shows that the purified happyase* used in the first two experiments was actually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation and the two experiments repeated, the measured Vmax in (a) is increased to 4.8 uM/s, and the measured Km in (b) is now 15 uM. Based on this information, can you figure out what type of inhibitor is ANGER? (Use table 6.9 at the end of the…
G6P(ag) F6P(aq) AG°=+1.7kJ/mol at 25 °C Consider the reaction: Estimate the fraction of F6P (Fructose 6 Phosphate) in equilibrium with G6P (Glucose 6 Phosphate) at 25 °C, where the fraction is defined as [F6P]/([F6P]+[G6P]). Show ALL your work.
Write a balanced equation for each of the following reactions or reactionsequences.(a) The reaction catalyzed by PFK-2(b) The conversion of 2 moles of oxaloacetate to glucose(c) The conversion of glucose to UDP-Glc(d) The conversion of 2 moles of glycerol to glucose(e) The conversion of 2 moles of malate to glucose-6-phosphate
Using Figure 1.3 of the Introduction as an example, a) draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). HAN+-CH- COOH (CH2)4 NH°+ b) indicate the numerical pa value of each equilibrium reaction, and which ionizable group is being dissociated in each step. c) indicate the net charge of the amino acid at each step and identify the zwitterion. d) Calculate the pI of this amino acid (show the calculation). e) What would be the predominant ionization states of this amino acid at physiological pH (7.4) and at this pH, what would the ratio of these two states be (show the calculation)?
In another key reaction in glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized into glyceraldehyde-3-phosphate (GAP): CH,OH | C=0 НС — ОН AG" = +7.5 kJ/mol CH,OPO,?- CH,OPO,- DHAP GAP Because AG° is positive, the equilibrium lies to the left. (a) Calculate the equilibrium constant, and the equilibrium fraction of GAP from the above, at 37 °C. (b) In the cell, depletion of GAP makes the reaction proceed. What will AG be if the concentration of GAP is always kept at 1/100 of the concentration of DHAP?
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Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD what are the reactants and what are the products is this reaction spontaneous? How do you know? Is energy released or consumed by this reaction? If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneous
draw all the structures of the tribasic amino acid lysine involved in the equilibrium reactions that would take place during titration against NaOH, starting with the fully protonated form below (draw the R-group in full). H;N+- CH - COOH (CH2)4 NH3+
a) The equilibrium reaction for the aqueous dissociation of acetic acid is shown below. CH3COOH(aq) = CH3COO-(aq) + H+ (aq) Given the data in the table below and your knowledge of the "chemical standard state" (X) and the “biochemical standard state” (Xº'), answer parts a) to e). c) For the dissociation of acetic acid at 298.15 K, calculate AG and the corresponding pK₁. b) Even though by definition, AfG©(H+ (aq)) = 0 and_AƒGº¹(H+(aq)) = 0, these are different physical quantities. What precisely does each represent? Calculate at 298.15 K, AG' for CH3COOH(aq) and CH3COO¯(aq). Gibbs free energy of formation, in units of kJ mol-¹, at T = 298.15 K AfGe A¢G° -396.5 -369.3 0 CH3COOH(aq) CH3COO- (aq) H+ (aq) d) For the dissociation of acetic acid at 298.15 K, calculate ArGº¹. LOXF 0 Finally, using the formula to convert between standard states, show that that your calculated values of AG and A.Gº are in agreement. jonly this

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