Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 1, Problem 4P
Interpretation Introduction
(a)
Interpretation:
To determine if the process follows the second law of
Concept introduction:
According to the second law of thermodynamics, the entropy of the entire universe increases with the time. Here, the universe is taken as an isolated system. Moreover, it is also said that the entropy change of the universe can never be negative. According to this law,
Interpretation Introduction
(b)
Interpretation:
To determine if the process follows the second law of thermodynamics or not.
Concept introduction:
According to the second law of thermodynamics, the entropy of the entire universe increases with the time. Here, the universe is taken as an isolated system. Moreover, it is also said that the entropy change of the universe can never be negative. According to this law,
Interpretation Introduction
(c)
Interpretation:
To determine if the process follows the second law of thermodynamics or not.
Concept introduction:
According to the second law of thermodynamics, the entropy of the entire universe increases with the time. Here, the universe is taken as an isolated system. Moreover, it is also said that the entropy change of the universe can never be negative. According to this law,
Interpretation Introduction
(d)
Interpretation:
To determine if the process follows the second law of thermodynamics or not.
Concept introduction:
According to the second law of thermodynamics, the entropy of the entire universe increases with the time. Here, the universe is taken as an isolated system. Moreover, it is also said that the entropy change of the universe can never be negative. According to this law,
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Analysis of the Temperature-Dependent Term of the rate of reaction
Provide at least 3 chemical equations with a given activation energy and frequency factor. (endothermic reactions, exothermic reactions, reactions with high and low Eact , reactions with catalyst)
provide equation problems only. no need to solve it.
kcat = ?
an enzyme has an aspartic acid in the active site with a pKa = 4.0 and the kcat for this enzyme is directly proportional to the fraction of this side chain that is ionized. If the kcat at pH = 4.0 is 52.9x103 s-1 what is the kcat for this enzymes at pH 3.5
multiple choice, choose the correct answer
Under which of the following conditions would an enzyme fail to be accurately described by the M-M equation:1. kcat >> k1 or k-12. In the presence of a negative allosteric effector3. At low concentrations, the reaction is first order with respect to substrate concentration4. At high concentrations the reaction is zero order with respect to substrate
Chapter 1 Solutions
Biochemistry
Ch. 1 - Prob. 1PCh. 1 - Prob. 2PCh. 1 - Prob. 3PCh. 1 - Prob. 4PCh. 1 - Prob. 5PCh. 1 - Prob. 6PCh. 1 - Prob. 7PCh. 1 - Prob. 8PCh. 1 - Prob. 9PCh. 1 - Prob. 10P
Ch. 1 - Prob. 11PCh. 1 - Prob. 12PCh. 1 - Prob. 13PCh. 1 - Prob. 14PCh. 1 - Prob. 15PCh. 1 - Prob. 16PCh. 1 - Prob. 17PCh. 1 - Prob. 18PCh. 1 - Prob. 19PCh. 1 - Prob. 20PCh. 1 - Prob. 21PCh. 1 - Prob. 22PCh. 1 - Prob. 23PCh. 1 - Prob. 24PCh. 1 - Prob. 25PCh. 1 - Prob. 26PCh. 1 - Prob. 27PCh. 1 - Prob. 28PCh. 1 - Prob. 29PCh. 1 - Prob. 30PCh. 1 - Prob. 31PCh. 1 - Prob. 32PCh. 1 - Prob. 33PCh. 1 - Prob. 34PCh. 1 - Prob. 35PCh. 1 - Prob. 36P
Knowledge Booster
Similar questions
- BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Which of the following best describes the transition state of a catalyzed reaction? A. higher in energy than that of an uncatalyzed reaction B. lower in energy than that of an uncatalyzed reaction C. bound very weakly to the catalyst D. lower energy than the reaction substratearrow_forwardChymotrypsin information about enzyme? Trivial/Common Name Systematic (EC) name and number Chemical reaction catalyzed Metabolic pathway Function and cellular localization Size (kDa) and structure (tertiary and quaternary) pH stability Kinetic properties (Km- and Kcat value/s for natural substrates) Stability and potential inhibitorsarrow_forward?? = ??A + log [? -]/[??] An enzyme uses histidine as a general acid catalyst. If the active site histidine has a pKa of 6.0, what percentage of the enzyme is active at pH 7.0? a. 1.0 %b. 9.1 % c. 45 %d. 55 % e. 91 %f. 99 % Please break down every step of the HH equation in as much detail as possible and explain why the answer is correct from a logical standpoint.arrow_forward
- Entropy increase A) with every reaction B) only in open systems C) only under certain reaction conditions D) only in the physical world. This cannot happen in cells otherwise cells would lose their needed energyarrow_forwardWhy is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!arrow_forwardThe decomposition of crystalline N2O5 N2O5(s) → 2NO2(g) + 1/2O2(g) is an example of a reaction that is thermodynamically favored, even though it absorbs heat. At 25 °C we have the following values for the standard state enthalpy and free energy changes of the reaction: ∆H° = +109.6 kJ/mol ∆G° = -30.5 kJ/mol (a) Calculate ∆S ° at 25 °C. (b) Why is the entropy change so favorable for this reaction?arrow_forward
- Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. The Michaelis-Menten Constant (Km) of an enzyme is equal to the enzyme concentration at which the initial velocity of the reaction is one half of maximum velocity (Vmax).arrow_forwardCalculate the Gibbs free energy change (G) for the following chemical reaction: glutamate + NH3 glutamine + H2OThe reaction occurs at 293 K, the change in heat (H) = 4103 cal, and the change in entropy (S) = 2.4 cal/K.arrow_forward9:34 AM You sent Help me with this one Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…arrow_forward
- 1- ATP consider as an important molecule in metabolism, because : A) It is one of the four building blocks for DNA synthesis.B) It provides energy coupling between exergonic and endergonic reactions.C) Its terminal phosphate group contains a strong covalent bond that, when hydrolyzed, releases free energy.D) Its hydrolysis provides an input of free energy for exergonic reactions.E) Its terminal phosphate bond has higher energy than the other two. 2- How many ATP yield from complete oxidation of glucose to carbon dioxide and water: A) 38 B) 32C) 2D) 8E)24arrow_forwardIf an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.arrow_forwardHello, For the image included: A) Which of the following statements are true of the malate dehydrogenase reaction in biochemical standard conditions? Choose all that apply. Group of answer choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium B) If the concentration of oxaloacetate is 107 times lower than the concentration of malate. Is the reaction spontaneous? Assume biochemical standard conditions. Group of answer choices No, because RTlnQ is very positive Yes, because RTlnQ is very positive No, because RTlnQ is very…arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning