ATP Synthase contains with in it one of the most conserved residues in a protein we know. Asp 61. This is the amino acid that carries the proton. a. Why would this residue be so highly conserved? What would happen if a mutation occurred that would change Asp to Ala? b. At the end of one spin of ATP synthase when the proton is in a position to leave to the intermembrane space the Asp comes into close contact with another very highly conserved residue Arg 210. Explain how this Arg residue could help the proton attached to Asp to leave. Hint think pKa Answer both parts with good explanation

ATP Synthase contains with in it one of the most conserved residues in a protein we know. Asp 61. This is the amino acid that carries the proton. a. Why would this residue be so highly conserved? What would happen if a mutation occurred that would change Asp to Ala? b. At the end of one spin of ATP synthase when the proton is in a position to leave to the intermembrane space the Asp comes into close contact with another very highly conserved residue Arg 210. Explain how this Arg residue could help the proton attached to Asp to leave. Hint think pKa Answer both parts with good explanation

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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V-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits and ATPIADP + Pj of the F-class synthase. Which of the following associations between the conformation of the beta subunit and ATP/ADP + P¡ is correct for V- Binding Change Mechanism loose binding ADP+P ATP ATP class pumps? C repeat ADP + P, ADP АТР tight binding АТР +P оpen АТР O The open conformation releases ATP. Hydrolysis of ATP to ADP + P¡ drives the change from tight to loose. O Binding of ADP + P¡ drives change from open to loose. Hydrolysis of ATP to ADP + Pj drives the change from open to loose.
The compound below, doxorubicin, is a substrate for p-glycoprotein. Cancer cells with a higher expression of P-gp (more P-gp protein per cell) than normal cells were treated with doxorubicin. What would be the expected observation? o= 0= OH O OH HCI OH -OH NH₂ & OH more doxorubicin inside the cell doxorubicin would be oxidized doxorubicin would have more cytotoxic effect on these cancer cells less doxorubicin inside the cell
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these condi- tions. The energy charge is the concentration of ATP plus half the concen- tration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
Many types of cells are able to use membrane-spanning transport proteins and a source of energy to drive the active transport of glucose across the cell membrane. Leť's consider a specific protein that is able to transport (from outside the cell into the cytoplasm) one molecule of glucose for each molecule of ATP the protein hydrolyzes. The details of this process are not important for this problem except that you can treat it like equilibrium process. The overall reaction and the associated AG at 298 K for this process are given below. Glc(out) + ATP + H20 = Glc(in) + ADP + P at T = 298 K, AG = -31.3 kJ mol-1 Additional Information: • P. is "inorganic phosphate" (i.e. PO4²- & related species). At equilibrium, [P] = 3 x 10-3 M. • The cell maintains a ratio of ATP to ADP of about 20 (i.e. [ATP]/[ADP] = 20). • The maximum ratio of [Glc(in)] to [Glc(out)] occurs when the system is at equilibrium. a) Write an expression for the equilibrium constant for this process. b) Your expression for…
The ATP hydrolysis reaction (shown below) has a AG of -31 kJ mol-1. NH2 NH2 Do you predict that AS is positive or negative for this reaction. Explain in one sentence. а. .N H20 -OCH2 OCH2 Energy Phosphate ion ÓH ÓH Adenosine triphosphate (ATP) Adenosine diphosphate (ADP) b. How does the hydrophobic effect contribute to the AS you predicted in part a. Make sure to discuss the ordering of water molecules in your answer. Include a minimum of 3 sentances in your explaination.
The enzyme mutase which is important for the synthetic of tyrosine and phenylalanine in saccharomyces cerevisiae has been studied as an example of an allosteric enzyme. Tyrosine acts as a negative effector for this enzyme. What effects would you see on the action of the enzyme were you to increase the concentration of tyrosine? The chorismate mutase would shift to its R conformation The curve showing the kinetics or chorismate mutase would shift to the right The curve showing the kinetics of chorismate mutase would shift to the left The chorismate mutase would become saturated more rapidly
a. Protein X can be phosphorylated. Why would the phosphorylated form of protein X elute AFTER the unphosphorylated form from an ANION exchange column? Please describe in terms of: The chemical properties of phosphorylation modification b. The chemical properties of an anion exchange column and how it works c. Why is an inhibitor that mimics the transition state more effective at enzyme inhibition than an inhibitor that mimics the substrate? d. Protein X can be covalently modified with many methyl groups. What two general properties would be different between the unmethylated protein versus the methylated protein?
The first step of the lysozyme reaction (catalytic mechanism) is shown in the figure below. Which statement regarding lysozyme is true? Glu 35 HO O(NAM) R (NAG) Asp 52 a. The local environment of Asp 52 significantly changes its pka. b. Glu 35 has an unusually low pKa due to its hydrophobic environment. c. Glu 35 provides acid/base assistance during catalysis. d. Glu 35 acts as a nucleophile during catalysis.
For each Pi released, the typical free energy of hydrolysis of inorganic polyphosphate (polyP) is about 20 kJ/mol. In Worked Example 13–2, we determined that synthesizing ATP from ADP and Pi requires roughly 50 kJ/mol of energy in a cell. Is it possible for a cell to manufacture ATP from ADP using polyphosphate? Give an explanation for your response.
The enzyme lysozyme kills certain bacteria by attacking a sugar called N-acetylglucosamine (NAG) in their cell walls. At an enzyme concentration of 2 × 10-6 M, the maximum rate for substrate (NAG) reaction, found at high substrate concentration, is 1 × 10-6 mol L¯'s1. The rate is reduced by a factor of 2 when the substrate concentration is reduced to 6 x 10-6 M. Determine the Michaelis-Menten constants Km and k, for lysozyme.
New anti-cancer agents are being developed that target fatty acid synthase (FASN) due to a requirement for lipid synthesis to promote tumor cell replication. Describe why an enzyme inhibitor targeted to the following sites would or would not work to inhibit lipid synthesis. Explain your answer. If you’re not sure whether it will work, make an argument for and against it working. ACP site on FASN The dimer interface between monomers of FASN Targeting FASN to mitochondrial matrix
Creatine is a popular dietary supplement. What is the biochemical rationale for the use of creatine? It would serve as an electron donor to support reductive biosyntheses required to sustain cellular function. It would promote the movement of ions through ion channels and thus power the synthesis of ATP during exercise. It would be converted into creatine phosphate and thus serve as a rapid means of replenishing ATP during muscle contraction. O It would directly serve as an electron carrier to support the oxidation of fuel molecules and thus energy production. What type of exercise would benefit most from creatine supplementation? O a long-distance run a leisurely walk yoga O sprinting