![OWLv2 with Student Solutions Manual eBook for Ebbing/Gammon's General Chemistry, 11th Edition, [Instant Access], 4 terms (24 months)](https://www.bartleby.com/isbn_cover_images/9781305864900/9781305864900_largeCoverImage.jpg)
Videos
Adenosine triphosphate, ATP, is used as a free-energy source by biological cells. (See the essay on page 624.) ATP hydrolyzes in the presence of enzymes to give ADP:
Consider a hypothetical biochemical reaction of molecule A to give molecule B:
Calculate the ratio [B]/[A] at 25°C at equilibrium.
Now consider this reaction “coupled” to the reaction for the hydrolysis of ATP:
If a cell maintains a high ratio of ATP to ADP and H2PO4− by continuously making ATP, the conversion of A to B can be made highly spontaneous. A characteristic value of this ratio is
Calculate the ratio [B][A] in this case and compare it with the uncoupled reaction. Compared with the uncoupled reaction, how much larger is this ratio when coupled to the hydrolysis of ATP?
Want to see the full answer?
Check out a sample textbook solution
Chapter 18 Solutions
OWLv2 with Student Solutions Manual eBook for Ebbing/Gammon's General Chemistry, 11th Edition, [Instant Access], 4 terms (24 months)
- U Consider the following graph containing line plots for the moles of Product 1 versus time (minutes) and the moles of Product 2 versus time in minutes. Choose all of the key terms/phrases that describe the plots on this graph. Check all that apply. ▸ View Available Hint(s) Slope is zero. More of Product 1 is obtained in 12 minutes. Slope has units of moles per minute. plot of minutes versus moles positive relationship between moles and minutes negative relationship between moles and minutes Slope has units of minutes per moles. More of Product 2 is obtained in 12 minutes. can be described using equation y = mx + b plot of moles versus minutes y-intercept is at (12,10). y-intercept is at the origin. Product Amount (moles) Product 1 B (12,10) Product 2 E 1 Time (minutes) A (12,5)arrow_forwardSolve for x, where M is molar and s is seconds. x = (9.0 × 10³ M−². s¯¹) (0.26 M)³ Enter the answer. Include units. Use the exponent key above the answer box to indicate any exponent on your units. ▸ View Available Hint(s) ΜΑ 0 ? Units Valuearrow_forwardLearning Goal: This question reviews the format for writing an element's written symbol. Recall that written symbols have a particular format. Written symbols use a form like this: 35 Cl 17 In this form the mass number, 35, is a stacked superscript. The atomic number, 17, is a stacked subscript. "CI" is the chemical symbol for the element chlorine. A general way to show this form is: It is also correct to write symbols by leaving off the atomic number, as in the following form: atomic number mass number Symbol 35 Cl or mass number Symbol This is because if you write the element symbol, such as Cl, you know the atomic number is 17 from that symbol. Remember that the atomic number, or number of protons in the nucleus, is what defines the element. Thus, if 17 protons are in the nucleus, the element can only be chlorine. Sometimes you will only see 35 C1, where the atomic number is not written. Watch this video to review the format for written symbols. In the following table each column…arrow_forward
- need help please and thanks dont understand only need help with C-F Learning Goal: As discussed during the lecture, the enzyme HIV-1 reverse transcriptae (HIV-RT) plays a significant role for the HIV virus and is an important drug target. Assume a concentration [E] of 2.00 µM (i.e. 2.00 x 10-6 mol/l) for HIV-RT. Two potential drug molecules, D1 and D2, were identified, which form stable complexes with the HIV-RT. The dissociation constant of the complex ED1 formed by HIV-RT and the drug D1 is 1.00 nM (i.e. 1.00 x 10-9). The dissociation constant of the complex ED2 formed by HIV-RT and the drug D2 is 100 nM (i.e. 1.00 x 10-7). Part A - Difference in binding free eenergies Compute the difference in binding free energy (at a physiological temperature T=310 K) for the complexes. Provide the difference as a positive numerical expression with three significant figures in kJ/mol. The margin of error is 2%. Part B - Compare difference in free energy to the thermal…arrow_forwardneed help please and thanks dont understand only need help with C-F Learning Goal: As discussed during the lecture, the enzyme HIV-1 reverse transcriptae (HIV-RT) plays a significant role for the HIV virus and is an important drug target. Assume a concentration [E] of 2.00 µM (i.e. 2.00 x 10-6 mol/l) for HIV-RT. Two potential drug molecules, D1 and D2, were identified, which form stable complexes with the HIV-RT. The dissociation constant of the complex ED1 formed by HIV-RT and the drug D1 is 1.00 nM (i.e. 1.00 x 10-9). The dissociation constant of the complex ED2 formed by HIV-RT and the drug D2 is 100 nM (i.e. 1.00 x 10-7). Part A - Difference in binding free eenergies Compute the difference in binding free energy (at a physiological temperature T=310 K) for the complexes. Provide the difference as a positive numerical expression with three significant figures in kJ/mol. The margin of error is 2%. Part B - Compare difference in free energy to the thermal…arrow_forwardPlease correct answer and don't used hand raitingarrow_forward
- need help please and thanks dont understand a-b Learning Goal: As discussed during the lecture, the enzyme HIV-1 reverse transcriptae (HIV-RT) plays a significant role for the HIV virus and is an important drug target. Assume a concentration [E] of 2.00 µM (i.e. 2.00 x 10-6 mol/l) for HIV-RT. Two potential drug molecules, D1 and D2, were identified, which form stable complexes with the HIV-RT. The dissociation constant of the complex ED1 formed by HIV-RT and the drug D1 is 1.00 nM (i.e. 1.00 x 10-9). The dissociation constant of the complex ED2 formed by HIV-RT and the drug D2 is 100 nM (i.e. 1.00 x 10-7). Part A - Difference in binding free eenergies Compute the difference in binding free energy (at a physiological temperature T=310 K) for the complexes. Provide the difference as a positive numerical expression with three significant figures in kJ/mol. The margin of error is 2%. Part B - Compare difference in free energy to the thermal energy Divide the…arrow_forwardPlease correct answer and don't used hand raitingarrow_forwardPlease correct answer and don't used hand raitingarrow_forward
- Can you tell me if my answers are correctarrow_forwardBunsenite (NiO) crystallizes like common salt (NaCl), with a lattice parameter a = 4.177 Å. A sample of this mineral that has Schottky defects that are not supposed to decrease the volume of the material has a density of 6.67 g/cm3. What percentage of NiO molecules is missing? (Data: atomic weight of Ni: 58.7; atomic weight of O: 16).arrow_forwardA sample of aluminum (face-centered cubic - FCC) has a density of 2.695 mg/m3 and a lattice parameter of 4.04958 Å. Calculate the fraction of vacancies in the structure. (Atomic weight of aluminum: 26.981).arrow_forward
Chemistry: The Molecular ScienceChemistryISBN:9781285199047Author:John W. Moore, Conrad L. StanitskiPublisher:Cengage Learning
Chemistry: Principles and PracticeChemistryISBN:9780534420123Author:Daniel L. Reger, Scott R. Goode, David W. Ball, Edward MercerPublisher:Cengage Learning
Chemistry: Principles and ReactionsChemistryISBN:9781305079373Author:William L. Masterton, Cecile N. HurleyPublisher:Cengage Learning
Chemistry & Chemical ReactivityChemistryISBN:9781337399074Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage Learning
Chemistry & Chemical ReactivityChemistryISBN:9781133949640Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage Learning
World of Chemistry, 3rd editionChemistryISBN:9781133109655Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCostePublisher:Brooks / Cole / Cengage Learning