EBK FUNDAMENTALS OF GENERAL, ORGANIC, A
8th Edition
ISBN: 8220102895805
Author: Peterson
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Videos
Question
Chapter 2, Problem 2.38AP
Interpretation Introduction
Interpretation:
Number of carbon atoms of
Concept introduction:
Number of moles can be calculated by using following formula,
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct
phosphorylation of glucose by P, is described by the equation
Glucose + P → glucose 6-phosphate + H₂O AG' = 13.8 kJ/mol
In principle, at least, one way to increase the concentration of glucose 6-phosphate (G6P) is to drive the equilibrium reaction to
the right by increasing the intracellular concentrations of glucose and Pj.
The maximum solubility of glucose is less than 1 M, and the normal physiological concentration of G6P is 250 μM. Assume a
fixed concentration of P, at 4.8 mM. The calculated value of K'cq is 4.74 × 10-³ M-¹.
Calculate the intracellular concentration of glucose when the equilibrium concentration of glucose 6-phosphate is 250 μM, the
normal physiological concentration.
[glucose] =
10.99
Correct Answer
Would increasing the concentration of glucose be a physiologically reasonable way to increase the concentration
of G6P?
No. Because the concentration of P,…
Calculate the equilibrium constant for the phosphorylation of glucose to glucose 6-phosphate at 37.0 °C.
K'eq =
M-'
In the rat hepatocyte, the physiological concentrations of glucose and P, are maintained at approximately 4.8 mM. What is the
equilibrium concentration of glucose 6-phosphate (G6P) obtained by the direct phosphorylation of glucose by P.?
[G6P] =
Does this reaction represent a reasonable metabolic step for the catabolism of glucose? Why or why not?
Yes, because the value of AG" is positive.
No, because the K'eq is too large for the reaction to proceed in the forward direction.
Yes, because AG is negative at the calculated value of K'eq
No, because [G6P] is likely to be higher than the calculated value.
M
The pKa values for glutamic acid are 2.19, 9.67, 4.25. Sketch out the titration curve for this amino
acid and include all of the pKa values and the pl.
Chapter 2 Solutions
EBK FUNDAMENTALS OF GENERAL, ORGANIC, A
Ch. 2.1 - Prob. 2.1CIAPCh. 2.1 - For the Kanji character in the lower portion of...Ch. 2.2 - Use the list inside the front cover to identify...Ch. 2.3 - Prob. 2.2PCh. 2.3 - Prob. 2.3PCh. 2.3 - Prob. 2.4PCh. 2.4 - Prob. 2.5PCh. 2.4 - Prob. 2.6PCh. 2.4 - Prob. 2.7PCh. 2.4 - Prob. 2.8P
Ch. 2.4 - Prob. 2.9PCh. 2.5 - Prob. 2.10PCh. 2.5 - Prob. 2.11PCh. 2.5 - Prob. 2.12PCh. 2.5 - Prob. 2.13KCPCh. 2.5 - Prob. 2.3CIAPCh. 2.5 - Prob. 2.4CIAPCh. 2.6 - Prob. 2.14PCh. 2.7 - Prob. 2.15PCh. 2.7 - Write electron configurations for the following...Ch. 2.7 - Prob. 2.17PCh. 2.7 - Identify the atom with the following...Ch. 2.8 - Prob. 2.19PCh. 2.8 - Prob. 2.20PCh. 2.8 - Prob. 2.21PCh. 2.8 - Prob. 2.22KCPCh. 2.9 - Prob. 2.23PCh. 2.9 - Write electron-dot symbols for radon, lead, xenon,...Ch. 2.9 - Prob. 2.25PCh. 2.9 - Prob. 2.5CIAPCh. 2.9 - Prob. 2.6CIAPCh. 2 - Where on the following outline of a periodic table...Ch. 2 - Is the element marked in red on the following...Ch. 2 - Prob. 2.28UKCCh. 2 - What atom has the following orbital-filling...Ch. 2 - Use the following orbital-filling diagram to show...Ch. 2 - What four fundamental assumptions about atoms and...Ch. 2 - How do atoms of different elements differ?Ch. 2 - Prob. 2.33APCh. 2 - Prob. 2.34APCh. 2 - Prob. 2.35APCh. 2 - Prob. 2.36APCh. 2 - How many O atoms of mass 15.99 amu are in 15.99 g...Ch. 2 - Prob. 2.38APCh. 2 - What are the names of the three subatomic...Ch. 2 - Prob. 2.40APCh. 2 - Prob. 2.41APCh. 2 - Prob. 2.42APCh. 2 - Which of the following symbols represent isotopes...Ch. 2 - Prob. 2.44APCh. 2 - Prob. 2.45APCh. 2 - Prob. 2.46APCh. 2 - One of the most widely used isotopes in medical...Ch. 2 - Prob. 2.48APCh. 2 - Prob. 2.49APCh. 2 - Prob. 2.50APCh. 2 - Prob. 2.51APCh. 2 - Prob. 2.52APCh. 2 - Prob. 2.53APCh. 2 - Prob. 2.54APCh. 2 - Prob. 2.55APCh. 2 - For (a) rubidium (b) tungsten, (c) germanium, and...Ch. 2 - For (a) calcium, (b) palladium, (c) carbon, and...Ch. 2 - Prob. 2.58APCh. 2 - Prob. 2.59APCh. 2 - Prob. 2.60APCh. 2 - Prob. 2.61APCh. 2 - Prob. 2.62APCh. 2 - Prob. 2.63APCh. 2 - Prob. 2.64APCh. 2 - Prob. 2.65APCh. 2 - Prob. 2.66APCh. 2 - Prob. 2.67APCh. 2 - Prob. 2.68APCh. 2 - Prob. 2.69APCh. 2 - Prob. 2.70APCh. 2 - Prob. 2.71APCh. 2 - Determine the number of unpaired electrons for...Ch. 2 - Without looking back in the text, write the...Ch. 2 - Prob. 2.74APCh. 2 - Prob. 2.75APCh. 2 - Prob. 2.76APCh. 2 - Prob. 2.77APCh. 2 - Prob. 2.78APCh. 2 - Using n for the number of the valence shell and...Ch. 2 - What elements in addition to helium make up the...Ch. 2 - Prob. 2.81CPCh. 2 - What is the atomic number of the yet-undiscovered...Ch. 2 - Give the number of electrons in each shell for...Ch. 2 - Identify the highest-energy occupied subshell in...Ch. 2 - Prob. 2.85CPCh. 2 - Prob. 2.86CPCh. 2 - Germanium, atomic number 32, is used in building...Ch. 2 - Prob. 2.88CPCh. 2 - Prob. 2.89CPCh. 2 - What is wrong with the following electron...Ch. 2 - Prob. 2.91CPCh. 2 - Prob. 2.92CPCh. 2 - Prob. 2.93CPCh. 2 - Prob. 2.94CPCh. 2 - Prob. 2.95GPCh. 2 - Prob. 2.96GPCh. 2 - Prob. 2.97GPCh. 2 - Look again at the trends illustrated in Figures...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Calculate the isoelectronic point, pl, from the pKa values for histidine, arginine and asparagine.arrow_forwardThe free energy released by the hydrolysis of ATP under standard conditions is -30.5 kJ/mol. If ATP is hydrolyzed under standard conditions except at pH 5.0, is more or less free energy released? Why? More free energy is released because the increased [H+] stabilizes the negative charge on the ADP molecule. Less free energy is released because an acidic environment depletes cellular ATP levels. Less free energy is released because the reaction favors ATP production over hydrolysis due to the higher [H+] in solution. More free energy is released because the total cellular concentrations of ATP, ADP, and P; are greater at the lower pH. Correct Answerarrow_forwardConsider a system consisting of an egg in an incubator. The white and yolk of the egg contain proteins, carbohydrates, and lipids. If fertilized, the egg transforms from a single cell to a complex organism. How does the entropy change in both the system (developing chick) and suroundings (the egg environment) drive the irreversible process of chick development? ☐ The release of glucose from sucrose, which produces energy needed for chick development, decreases entropy in the surroundings. Chick development increases entropy in the system, which causes a concominant decrease in entropy in the surroundings. Carbohydrates, proteins, and lipids within the egg break down into CO2 and H2O, which increases entropy in the surroundings. Chick development decreases entropy in the system, but this is smaller than the concominant increase in entropy in the surroundings.arrow_forward
- The amino acid glycine is often used as the main ingredient of a buffer in biochemical experiments. The amino group of glycine, which has a pKa of 9.6, can exist either in the protonated form -NH or as the free base -NH2, because of the reversible equilibrium R-NH =R-NH₂ + H+ In what pH range can glycine be used as an effective buffer due to its amino group? pH 8.6 to pH 10.6 In a 0.1 M solution of glycine at pH 9.0, what fraction of glycine has its amino group in the -NH form? Correct Answer Correct Answer 45 How much 5 M KOH must be added to 1.0 L of 0.1 M glycine at pH 9.0 to bring its pH to 10.0? 10 mL When 99% of the glycine is in its -NH form, what is the numerical relation between the pH of the solution and the pKa of the amino group? pH = pKa - 2 Correct Answer Correct Answerarrow_forwardThe glycolytic enzyme Phosphofructokinase (PFK) catalyzes the following reaction: Fructose-6-phosphate (F6P) + ATP → Fructose-1,6-bisphosphate (F1,6BP) + ADP AG"=-14.2 kJ/mol This is considered the enzymatic step that commits a sugar substrate to glycolysis. a) Calculate the standard free energy of hydrolysis of fructose-1,6-bisphosphate. b) What is the equilibrium constant for this coupled reaction? c) ATP is a known inhibitor of PFK. If the cellular concentrations of ATP and ADP are 5 mM and 1.0mM respectively, and the concentrations of F6P and F1,6BP are 2mM, what is the free energy change of the system?arrow_forward2) Consider the following reaction: A + 2B 3C + D At equilibrium the concentration of the reactants and products are: [A] = 20.0 mM [C] = 3.0 mM [B] = 4.0 mM [D] = 50.0 mM Calculate (a) the equilibrium constant and (b) AG". Comment on which side of this reaction is more likely to occur.arrow_forward
- Glycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (NH), and the other for the carboxyl (-COOH) group. Therefore, it has two pK₁ values. The carboxyl group has a pK₁ of 2.34 and the α-amino group has a pK2 of 9.60. Glycine can exist in fully deprotonated (NH2-CH2-COO¯), fully protonated (NH3-CH2-COOH), or zwitterionic form (NH3-CH2-COO¯). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of that pH. fully deprotonated form NH2-CH2-COO- fully protonated form NH–CH,–COOH zwitterionic form NH–CH,−COO Answer Bank pH 7.0 pH 11.9 pH 6.0 pH 8.0 pH 1.0arrow_forwardThe AG of hydrolysis of a sugar phosphate (S-O-P) to the free sugar (S-OH) is -26.6 kJ/mol in a hypothetical cell in which the steady-state concentrations of sugar phosphate, free sugar, and inorganic phosphate are 1.0 mM, 0.20 mM, and 50.0 mM, respectively. S-O-P + H2O S-OH + Pi (a) What is the AG°' for this reaction? (b) In the cell, S-O-P is formed by the transfer of a phosphate group from ATP. What would the AG be for the transfer of the g-phosphate from ATP to this sugar (S-OH)? [AG for ATP hydrolysis is -31 kJ/mol.]arrow_forward1) Consider the reaction: A B + C (a) What is the Keg for this reaction? AG= -8.80 kJ/mol (b) The reverse reaction is initiated by creating a solution containing 20mM B, 1mM A and 150mM C. At the instant these are mixed, what is the free energy change associated with the reaction?arrow_forward
- What is the chemical importance of the negative charge on the phosphate group? Be asspecific as possible. In what ways might this negative charge have beenthermodynamically useful during the evolution of ATP-binding proteins?arrow_forwardOne prominent theory on life origins was that RNA enzymes came into existence early inthe prebiotic history of Earth and were able to do basic chemical catalyses. Eventually,this “RNA-world” was overtaken by the stability of DNA as an information carrier and thediversity of catalytic functions capable of being performed by polypeptides. Is the RNA world hypothesis is a well-founded model?arrow_forwardThe AG" of hydrolysis (ATP + H2O --> ADP + Pi) is -31.0 kJ/mol. Answer the following questions assuming that the steady-state concentrations in the cell are as indicated below. (Note: Steady-state refers to a non-equilibrium situation that exists due to a balance between reactions that supply and remove these substances.) [ADP] = 0.40 mM, [ATP] = 4.0 mM, and [Pi] = 40.0 mM a) Calculate the equilibrium constant for this reaction. b) What would the AG' for ATP hydrolysis be in the cell? c) Is this reaction at equilibrium in the cell? Briefly explain your answer.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Principles Of Radiographic Imaging: An Art And A ...Health & NutritionISBN:9781337711067Author:Richard R. Carlton, Arlene M. Adler, Vesna BalacPublisher:Cengage Learning
Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning
Anatomy & PhysiologyBiologyISBN:9781938168130Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark WomblePublisher:OpenStax College
Biology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage Learning
Principles Of Radiographic Imaging: An Art And A ...
Health & Nutrition
ISBN:9781337711067
Author:Richard R. Carlton, Arlene M. Adler, Vesna Balac
Publisher:Cengage Learning
Biology (MindTap Course List)
Biology
ISBN:9781337392938
Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher:Cengage Learning
Anatomy & Physiology
Biology
ISBN:9781938168130
Author:Kelly A. Young, James A. Wise, Peter DeSaix, Dean H. Kruse, Brandon Poe, Eddie Johnson, Jody E. Johnson, Oksana Korol, J. Gordon Betts, Mark Womble
Publisher:OpenStax College
Biology: The Dynamic Science (MindTap Course List)
Biology
ISBN:9781305389892
Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan
Publisher:Cengage Learning
GCSE Chemistry - Acids and Bases #34; Author: Cognito;https://www.youtube.com/watch?v=vt8fB3MFzLk;License: Standard youtube license