Choose one of the three questions to write afollow-up question for A & B.A. Pick oneQ1.1 - What is the difference between actual change in free energy (deltaG) and biochemical standard change in free energy (delta Gº) with regard tothe spontaneity of a given reaction in a living cell?Review of Enzyme Function and RegulationQ1.2 - Name three processes affecting enzyme bioavailability and threemechanisms controlling catalytic efficiency.Plants Harvest Energy from the SunQ1.3 - How do eukaryotic plants obtain energy at night to maintainsufficiently high levels of ATP?You must start a thread before you can read and reply to other threadsB. Pick oneIntroduction to Biochemical PrinciplesQ1.1 Hierarchical organization and chemical complexity can beexemplified by the Saguaro desert as the ecosystem. Provide an examplefor each of the other six hierarchies leading up to this ecosystem.Energy Conversion ProcessesQ1.2 The Second Law of Thermodynamics states that all spontaneousprocesses in the universe tend toward the dispersal of energy in theabsence of energy input, which leads to death for a living organism. Whatare the two sources of energy for an autotroph over a 24 hour period andwhat are the chemical processes involved in each?Structure and Function of WaterQ1.3 - Planetary scientists are searching for planets with water because itwill support our chemical life. Name three properties that make H20uniquely critical to life on Earth.

As you have mentioned, in both parts, one of the three questions has to be packed and solved. That's…

Answered: actual change in free energy

Science

Chemistry

actual change in free energy

Chemistry & Chemical Reactivity

10th Edition

ISBN:9781337399074

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions

Section14.7: Reaction Mechanisms

Problem 1.2ACP

See similar textbooks

Similar questions

List two ways that enzyme catalysis of a reaction is superior to normal conditions.
Most human enzymes function best in the temperature range of: a. 0C10C b. 10C25C c. 25C40C d. 40C55C
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
Calculate the equilibrium constant at 37oC for the reactionGlucose + 6O2 + 36ADP + 36Phospate → 6CO2+ 42H2O +36ATP ... ... ...Entropy change of Go= − 423 kcal/mole of Glucose
Enzyme kinctics a. How to determine Km and Vmax of a-glucosidase enzyme isolated from weathered rice b. Curcumin is expected to inhibit the activity of the a-glucosidase enzyme. How to determine the inhibitory activity of curcumin against a -glucosidase? c. If the results of experiment number 3b are known that curcumin can inhibit a -glucosidase, how to determine the type of inhibitor?
1. Calculation of AG from an Equilibrium Constant Calculate the standard free-energy change for each of the following metabolically important enzyme-catalyzed reactions, using the equilibrium constants given for the reactions at 25 °C and pH 7.0, R = 8.315 J/molK Aspartate aminotranterase (a)Glutamate + oxaloacetate 2 aspartate + a-ketoglutarate Keg-6.8 Triosephosphate isomerase (b)Dihydroxvacetonephosphate glyceraldehyde3phosphate Keg-0.0475 phosphofructokinase e fructose1,6-bisphosphate+ADP Keg=254 (c)Fructose6-phosphate + ATP
1. For an enzyme to catalyze a reaction, it must preferentially stabilize the transition state (TS) of the reaction. If an enzyme instead preferentially stabilizes the enzyme-substrate complex (ES), it fails to catalyze the reaction. Justify this observation using a reaction coordinate diagram (free energy (G) vs. reaction coordinate).
One of the important reactions in the biochemical pathway glycolysis is the reaction of glucose-6-phosphate (G6P) to form fructose-6-phosphate (F6P): G6P F6P AG-1.7 kJ Phosphoglucose Isomerase 6 CH2OPO, 2- H. CH2OPO3 ICH,OH H. H. HO. H. 1. H. HO. HO. H. 14 B OH H. H. HO. gluco se-6-phosphate fructo se-6-phosphate Standard thermodynamic conditions imply the concentrations of G6P and F6P to be 1 M, however, in a typical cell, they are not even close to these values. Calc kJ when the concentrations of G6P and F6P are 60.0 ×10M and 14.0 x10 M respectively, assume the temperature is 37 °C. (R = 8.314 J/K-mol) O a. -0.1 kJ Ob.-1.1 kJ Oc.-2.1 kJ O d.-3.1 kJ O e.-4.1 kJ
6) If we represent protein folding with the following equilibrium expression: Unfolded protein z folded protein The values of AH and AS° for the folding of lysozyme protein are -280 kJ/mol and -790 J/mol-K, respectively. a) Based on these values, calculate AG° for the folding process at 25 °C. b) At what temperature would you expect the unfolding process to become unfavorable?
Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP creatine + ATP at 37 °C, as it occurs in the cytosol of neurons, where [phosphocreatine] = 4.7 mM, [creatine] = 1.0 mM, [ADP] = 0.73 mm, and [ATP] = 2.6 mm. Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds AG = Phosphorylated compound phosphoenolpyruvate phosphocreatine ADP (→ ATP (→ AMP + P;) ADP + P₁) AG' (kJ/mol) -61.9 -43.0 -32.8 -30.5 kJ/mol
Which of the following statements is incorrect? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. Inhibitors affect the ability of enzymes to function. Enzymes decompose during the reaction that they catalyze. The typical biochemical reaction occurs more than one million times faster in the presence of an enzyme wF to the reaction without the enzyme. The catalytic function of enzymes is dependent on their three-dimensional structures
From the given activity, 1.) What is the effect of temperature to the enzyme? 2.) What are some generalizations and conclusions in this activity?