Problem 1:Calculate the hydrolysis of ATP at pH 7 at 37°C under steady state conditions in whichthe concentration of ATP, ADP and Pi are maintained at 10-³M, 10 M and 10-2M, respectively.The AG' of hydrolysis of ATP at pH 7 = -32,217 J/mole, R = 8.314 JK ¹mol-¹, T= 273 + 37 K.ATP ADP + Pi

In a general reaction such as: aA + bB ⇌ cC + dD At equilibrium (steady state), the concentration of…

Answered: Problem 1: Calculate the hydrolysis of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

Question: Determine the Km and Vmax for this enzyme/substrate combination. [Substrate] (mM) V0 (mM/min) 0.25 0.183 0.50 0.356 1.00 0.665 2.50 1.45 5.00 2.35 What is the concentration of substrate necessary to achieve a turnover rate of 1.00 mM/min?
ent Page Form Combine Files Protect Flatten File Ch. 7] PROBLEMS Share 390% Enzymes-2.pdf Help + < Problems 125 (142/434) Capture the ronction: Add Bookmark 7.1 The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmol 1¹¹): 5.0 Initial velocity (umol l´¹ min¯¹): 147 Calculate Km and Vmax 6.67 10.0 20.0 182 233 323 125 40.0 400
What is time constant ? The steel ball bearings of 40 mm diameter and initially at uniform temperature of 600 °C are quenched in an oil bath maintained at 50 °C temperature. The heat transfer coefficient between the ball bearing and oil is 325 W/m2-K and the thermodynamics properties of the bearing can be taken as : k 45 W/m-K and thermal diffusivity a = 1.25 x 10-5 m/s. Determine : The time duration for which bearing must remain in oil to attain 225 °C temperature. b. The instantaneous heat transfer rate from the bearings when they are first immersed in oil and when they reach 225 °C.
7.1 The following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmolr'): Initial velocity (umol I' min"): 6.67 182 10.0 20.0 40.0 147 233 323 400 Calculate Km and Vmax
PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme čoncentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) With 1 mmol I-B Uninhibited With 1 mmol l- A 0.684 50 20 1.08 0.653 0.468 10 1.43 1.01 0.649 0.476 0.374 0.311 5 1.02 0.363 0.798 0.657 3.3 0.296 2.5 0.250 2.0 0.549 Comment on these results. 8.2 The system investigated in problem 7.1 was investigated again under identical conditions but in the presence of an inhibitor, giving the following data: 40.0 6.67 10.0 156 20.0 Substrate conc" (mmol 1-1) Initial velocity (umol 1- min-1) 5.0 100 122 222 278 Determine the type of inhibition. If K, for this system is 2.9 mmol 1-', calculate the inhibitor concenträtion present.
how to calculate these? can you give me the steps or the equations for that? 2ul St.1 St.2 St.3 St.4 Absorbance 595nm 0.926 0.444 0.421 0.462 0.932 0.412 0.407 0.393 Ç Average Abs Corrected Abs 595nm 595nm 0.929 0.428 0.414 0.4275 0.5615 0.0605 0.0465 0.06 [Protein] (µg/ml) 103.98 11.20 8.61 11.11 Volume (ml) 20 40 8 4 [Total Protein] (ug) 2079.63 448.15 68.89 44.44
Problem 3 Is the protonation state of the tripeptide, Glu-Lys-Cys, as drawn below feasible? If so, at what pH? If not, why not? What is the isoelectric point for this tripeptide? O OH SH *H,N NH
10. Calculating AG in a Rat Liver Cell Calculate the free energy of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and P₁ concentrations are 3.4, 1.3, and 4.8 mM, respectively.
PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme čoncentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) With 1 mmol I-IB Uninhibited With 1 mmol I-1À 50 20 0.684 1.08 0.653 1.01 0.649 0.476 0.374 0.311 10 1.43 0.468 1.02 0.363 0.296 3.3 0.798 2.5 2.0 0.657 0.549 0.250 Comment on these results.
Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graph
Problem: Alcohol Dehydrogenase catalyzes the conversion of ethanol to acetaldehyde. This enzyme, in its active state, consists of a protein molecule and a zinc ion. On the basis of this information, identify the following for this chemical system. Substrate Apoenzyme Cofactor Holoenzyme
2.For question number 1 if a mixture was prepared containing 1 M Glucose 6-Phosphate and 0.001 M Glucose 1-Phosphate the ∆G for this reaction is: included question 1 however, need help with 2 and provided the option for the answer 1.What is the Keq for the conversion of Glucose 1-Phosphate to Glucose 6-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are 20.9 kJ/mol and 13.8 kJ/mol respectively?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS

Problem 1: Calculate the hydrolysis of ATP at pH 7 at 37°C under steady state conditions in which the concentration of ATP, ADP and Pi are maintained at 10 ³M, 10 M and 102M, respectively. The AG' of hydrolysis of ATP at pH 7 = -32,217 J/mole, R = 8.314 JK ¹mol-¹, T= 273 +37 K. ATP ADP + Pi