The protein unfolds at a transition temperature of 75 °C and the standard enthalpy of transition is 61 kJ mol-¹. Calculate the absolute molar entropy (S(353 K)) of the unfolded protein at 80°C, if Cp, folded = aT³ below 10K (a = 0.0257 J K-2 mol-¹), above 10K Cp, folded = 5.23 J K-¹ mol-¹ and Cp. unfolded= 6.28 kJ K-¹ mol-¹,.

The protein unfolds at a transition temperature of 75 °C and the standard enthalpy of transition is 61 kJ mol-¹. Calculate the absolute molar entropy (S(353 K)) of the unfolded protein at 80°C, if Cp, folded = aT³ below 10K (a = 0.0257 J K-2 mol-¹), above 10K Cp, folded = 5.23 J K-¹ mol-¹ and Cp. unfolded= 6.28 kJ K-¹ mol-¹,.

Chemistry: Principles and Reactions

8th Edition

ISBN:9781305079373

Author:William L. Masterton, Cecile N. Hurley

Publisher:William L. Masterton, Cecile N. Hurley

Chapter16: Spontaneity Of Reaction

Section: Chapter Questions

Problem 78QAP

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3. A particular protein heat denatures with a melting temperature Tm = 332 K with an enthalpy of unfolding, AHm = 372 kJmol-¹. (a) What is the entropy of unfolding in kJ mol-1 K-1 at Tm? (b) If ACp is 6.6 kJ mol-1 K-1, at what temperature does the free energy of unfolding (AG unfolding) have the greatest value (i.e. the native state is most stable)? (c) Calculate the value of AG and K at this temperature.
A direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically very demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. However, the value of AG'o for ATP hydrolysis can be calculated indirectly, from the equilibrium constants of two other enzymatic reactions having less favourable equilibrium constants: Glucose-6-phosphate + H20 = glucose + Pi K'eg = 271 (1) ATP + glucose = ADP + glucose-6-phosphate K'eg = 889 (2) Use this information to determine the value for AG'o for the hydrolysis of ATP at 25°C. Justify the method used.
Wheeler and Mathews (J. Biol. Chem. 287:31218–31222 (2012)) reportedthe NAD+ and NADH concentrations in yeast mitochondria as 20 mM and0.3 mM, respectively. Consider the malate dehydrogenase reaction, which is part of the citric acid cycle:malate + NAD+ → oxaloacetate + NADH + H+ ΔG∘' = +29.7 kJ/molIf malate concentration in yeast mitochondria is 0.4 mM, what is the maximum concentration of oxaloacetate needed to make the reaction exergonic at pH 7.0 and 37°C?
A key step in the biosynthesis of triglycerides (fats) is the conversion of glycerol to glycerol-1- phosphate by ATP: Mg2+ Glyserol (G) + ATP glyserol-1-phosphate (G-1-P) + ADP a-glycerol kinase At a steady state in the living cell, (ATP) = 10-³M and (ADP) 104 M. The maximum (equilibrium) value of the ratio (glycerol-1-P)/(glycerol) is observed to be 770 at 25 °C and pH=7. a. Calculate K and A,G° for the reaction. b. Using the value of AG° for the reaction ADP + Pi →ATP +H2O, together with the answer to part (a), calculate A:G° and K for the reaction: glycerol+ phosphate> glycerol-1-phosphate+ H2O
At 298K, the enthalpy of denaturation of hen egg white lysozyme is +217.6 kJ/mol, and the changein the constant pressure molar heat capacity resulting from denaturing this protein is +6.3 kJ/molK. Estimate the enthalpy of denaturation of this protein at 351 K (the melting temperature of hen egg white lysozyme at atmospheric pressure). (ans = +552 kJ/mol)
in a particular solution at 30 degrees celcius the ratio of beta-d-glucose to linear glucose is 320:1. Calculate gibbs free energy at standard state for conversion of linear to beta-d-glucose. (R=8.3145 J mol-1 K-1)
The glucose fermentation reaction is C6H12O6 (aq) → 2 C₂H5OH (aq) + 2 CO₂ (g), finding the summarized thermodynamic data in the following table: AHO (kJ mol-¹) AGO (kJ mol-¹) C6H12O6 (aq) C₂H5OH (aq) -1261,5 -914,5 -277,7 -174,8 CO2 (g) -393,5 -394,4 What is the free energy AG of this reaction at 25°C and justify if it is a spontaneous process. Indicate the entropy change AS at the same temperature.
Double-helix-formation entropy. For double-helix forma- tion, DG can be measured to be 254 kJ mol?1 (213 kcal mol?1) at pH 7.0 in 1 M NaCl at 258C (298 K). The heat released indicates an enthalpy change of 2251 kJ mol?1 (260 kcal mol?1). For this process, calculate the entropy change for the system and the entropy change for the surroundings.
17.) A protein's enthalpy of denaturation (AH) at its denaturation temperature is 80.9 kcal/mol. The protein's Tm is 68 °C, and its AC, is 1650 cal/(mol K). (a) Calculate AS (Tm), ASd(37 °C) and AS (15 °C). (b) At what temperature is AS = 0?
Calculate the equilibrium constant at 37oC for the reactionGlucose + 6O2 + 36ADP + 36Phospate → 6CO2+ 42H2O +36ATP ... ... ...Gibbs free energychange of Go= − 423 kcal/mole of Glucose
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3. Experimental Determination of AG for ATP Hydrolysis A direct measurement of the standard free- energy change associated with the hydrolysis of ATP is technically demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. The value of AGo can be calculated indirectly, however, from the equilibrium constants of two other enzymatic reactions having less favorable equilibrium constants: Glucose6-phosphate + H.O - glucose + Pi Keg 270 ATP+glueose > ADP + glucosE6-phosphate K eg 890 Using this information for equilibrium constants determined at 25 °C, calculate the standard free energy of hydrolysis of ATP.