Homework Answers
'R' state.
Deoxy Haemoglobin is 'T' state and fully loaded oxy Haemoglobin is 'R' state.
One molecule of haemoglobin can bind 4 oxyzen molecule.So one by one, oxyzen molecules bind to the deoxyhaemoglobin(T state) and thus oxyzen biases the equilibrium towards the 'R' state(fully oxy haemoglobin).
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7. Fill in the blanks Oxygen biases the equilibrium of hemoglobin towards the state.
For the following questions consider this equation for hemoglobin – oxygen equilibrium. Hb + 4O2⥤ Hb(O2)4...
For the following questions consider this equation for hemoglobin – oxygen equilibrium. Hb + 4O2⥤ Hb(O2)4 Carbon Monoxide (CO) bonds to hemoglobin approximately 230 times stronger than oxygen. How would you increase the bonding oxygen to a patient with carbon monoxide poisoning?
The binding of oxygen to hemoglobin in the blood involves the equilibrium reaction: Carbon monoxide replaces...
The binding of oxygen to hemoglobin in the blood involves the equilibrium reaction: Carbon monoxide replaces oxygen in oxygenated hemoglobin according to the reaction: HbO2(aq) + CO(aq)HbCO(aq) + O2(aq) a. If the normal pH of blood is controlled within a range of 7.35 to 7.45. If the pKw is 13.63, what is the normal range of [H+] and [OH- b. What would happen if oxygenated hemoglobin became too acidic? c. Use the reaction and associated equilibrium constants at body temperature...
Which of the following is NOT an indication that the binding of oxygen to hemoglobin is...
Which of the following is NOT an indication that the binding of oxygen to hemoglobin is cooperative? a. Oxygen binding of one subunit induces a shift of the other hemoglobin subunits from the T state to the R state. b. A plot of hemoglobin’s fractional saturation against partial pressure of oxygen (Y versus pO2), is sigmoidal rather than hyperbolic. c.Hemoglobin has four subunits, each of which can bind oxygen. d.The Hill coefficient, n, is greater than 1.0.
If the oxygenation of hemoglobin has an equilibrium constant (Kc) of 0.45, and the initial concentration...
If the oxygenation of hemoglobin has an equilibrium constant (Kc) of 0.45, and the initial concentration of hemoglobin is 0.010 M and initial concentration of oxygen is 0.020M, what is the equilibrium concentration of oxygenated hemoglobin? Hemoglobin + O2 --> Hemoglobin-O2 0.000089M 0.0099M 0.020M 0.20M
Bisphosphoglycerate (BPG) is a byproduct of glycolysis. It can bind to the deoxy state of hemoglobin...
Bisphosphoglycerate (BPG) is a byproduct of glycolysis. It can bind to the deoxy state of hemoglobin but not the oxy state. Complete the sentence to explain how you expect BPG to shift the Hb-oxygen binding equilibrium. Addition of BPG will _______ because the system needs to compensate for _______ in _________ due to BPG.
Oxygen-Proton Exchange in Hemoglobin 11.0 10.0 As shown in the graph, hemoglobin exchanges oxygen and protons...
Oxygen-Proton Exchange in Hemoglobin 11.0 10.0 As shown in the graph, hemoglobin exchanges oxygen and protons due to an inverse relationship between oxygen binding and proton binding known as the Bohr effect. The binding of oxygen to hemoglobin causes a conformational change that disrupts salt bridges, making oxyhemoglobin more acidic than deoxyhemoglobin. For purposes of calculation, hemoglobin can be modeled as a simple monoprotic buffer, dissociating one proton per subunit as illustrated in the graph and equilibrium equations. Tissues -...
10. 'Circle’ the correct answer (option1/option2/option3) and Fill in the Blanks in the following statements. (4...
10. 'Circle’ the correct answer (option1/option2/option3) and Fill in the Blanks in the following statements. (4 marks) I. The first crystal structure of a protein was the structure of II. The prosthetic group is located inside this protein, is the Iron/ Heme/ Pyrrole ring(s). III. In the quaternary structure of a protein molecule, each polypeptide chain is called the IV. The overall structure of hemoglobin can be represented as V. The binding pattern of O, in hemoglobin exhibits free VI....
Fill in the blanks regarding DNA hybridization (5 marks): a. Increasing temperature towards the Tm duplex...
Fill in the blanks regarding DNA hybridization (5 marks): a. Increasing temperature towards the Tm duplex hybridization. b. Adding organic solvent to a sample of hybridized dsDNA temperature Doubling the amount of dsDNA in a sample 1. the stringency of DNA the melting the Tm and C. the A260 value d. If A250 1.0 in a dsDNA sample under standard conditions, and then the sample is incubated at its Tm, the A2s0 Value will A260 change by? BONUS: what percentage...
1 Which state of hemoglobin, R or T, is stabilized by BPG, and how does PBG...
1 Which state of hemoglobin, R or T, is stabilized by BPG, and how does PBG affect oxygen binding to hemoglobin? 2 Compare the binding of hemoglobin to oxygen and carbon dioxide. This question requires you to compare side by side oxygen and carbon dioxide binding to hemoglobin, not to define them independently
In a real hemoglobin molecule, the tendency of oxygen to bind to a heme site increases...
In a real hemoglobin molecule, the tendency of oxygen to bind to a heme site increases as the other three heme sites become occupied. To model this effect in a simple way, imagine that a hemoglobin molecule has just two sites, either or both of which can be occupied. This system has four possible states (with only oxygen present). Take the energy of the unoccupied state to be zero, the energies of the two singly occupied states to be -0.55...
The binding of oxygen to hemoglobin in the blood involves the equilibrium reaction: Carbon monoxide replaces oxygen in oxygenated hemoglobin according to the reaction: HbO2(aq) + CO(aq)HbCO(aq) + O2(aq) a. If the normal pH of blood is controlled within a range of 7.35 to 7.45. If the pKw is 13.63, what is the normal range of [H+] and [OH- b. What would happen if oxygenated hemoglobin became too acidic? c. Use the reaction and associated equilibrium constants at body temperature...
Oxygen-Proton Exchange in Hemoglobin 11.0 10.0 As shown in the graph, hemoglobin exchanges oxygen and protons due to an inverse relationship between oxygen binding and proton binding known as the Bohr effect. The binding of oxygen to hemoglobin causes a conformational change that disrupts salt bridges, making oxyhemoglobin more acidic than deoxyhemoglobin. For purposes of calculation, hemoglobin can be modeled as a simple monoprotic buffer, dissociating one proton per subunit as illustrated in the graph and equilibrium equations. Tissues -...
10. 'Circle’ the correct answer (option1/option2/option3) and Fill in the Blanks in the following statements. (4 marks) I. The first crystal structure of a protein was the structure of II. The prosthetic group is located inside this protein, is the Iron/ Heme/ Pyrrole ring(s). III. In the quaternary structure of a protein molecule, each polypeptide chain is called the IV. The overall structure of hemoglobin can be represented as V. The binding pattern of O, in hemoglobin exhibits free VI....
Fill in the blanks regarding DNA hybridization (5 marks): a. Increasing temperature towards the Tm duplex hybridization. b. Adding organic solvent to a sample of hybridized dsDNA temperature Doubling the amount of dsDNA in a sample 1. the stringency of DNA the melting the Tm and C. the A260 value d. If A250 1.0 in a dsDNA sample under standard conditions, and then the sample is incubated at its Tm, the A2s0 Value will A260 change by? BONUS: what percentage...
In a real hemoglobin molecule, the tendency of oxygen to bind to a heme site increases as the other three heme sites become occupied. To model this effect in a simple way, imagine that a hemoglobin molecule has just two sites, either or both of which can be occupied. This system has four possible states (with only oxygen present). Take the energy of the unoccupied state to be zero, the energies of the two singly occupied states to be -0.55...
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