ZuoTi.Pro
Question

The Bohr Effect results in the release of protons when O2 binds to Hb. The beta...

The Bohr Effect results in the release of protons when O2 binds to Hb. The beta subunit of Hb possesses a terminal histidine with a pka of 7.1 in the T state. What is the ratio of protonated to unprotonated histidine at pH 7.4? When the conformation of Hb changes to the R state, does the pka of the histidine increase or decrease? What would cause this change in pka?

science   chemistry   
0 0
Add a comment Improve this question Transcribed image text
Next > < Previous
Sort answers by oldest

Homework Answers

Answer #1

0 0
Add a comment
Know the answer?
Add Answer to:
The Bohr Effect results in the release of protons when O2 binds to Hb. The beta...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Log In

Sign Up

Not the answer you're looking for? Ask your own homework help question. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions

  • 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 -...

  • In the Bohr effect, protonation of the imidazolium rings of the C-terminal rings of the C-terminal...

    In the Bohr effect, protonation of the imidazolium rings of the C-terminal rings of the C-terminal residues (His 126B) of the hemoglobin's two B chains is responsible for around 40% of the .60 mole of H+ that combine with Hb on the release of 1.00 mole of O2 at pH 7.40. Assuming that this imidazolium group has pKa = 7.10 in R-state oxyHb, what is its pKa value in T-state deoxyHb? (Hint: the pH of the blood - because it's...

  • Regarding the effects of the affinity of hemoglobin when 2,3-biphosphoglycerate (BPG) is regulating, analyze the biochemical...

    Regarding the effects of the affinity of hemoglobin when 2,3-biphosphoglycerate (BPG) is regulating, analyze the biochemical mechanisms that occur to cause the catch and release of oxygen in this manner. Which of the following structural changes occur when deoxyhemoglobin binds to oxygen? Choose the two correct answers and briefly explain why the other two are incorrect: 1.) The proximal histidine (His F8) moves helix F towards the planar heme. 2.) The heme releases CO2 from the other subunits. 3.) A...

  • In the Bohr effect, the protonation of the N-terminal amino groups in the alpha chains of...

    In the Bohr effect, the protonation of the N-terminal amino groups in the alpha chains of hemoglobin is responsible for 30% of the 0.6moles of H+ that combine with hemoglobin when 1 mole of O2 is released at pH 7.4. Assuming that the N-terminial amino groups have a pKeq of 7.0 in the R state, what is the pKeq in the T state?

  • For the video response portion of this assignment, your job will be to state what would happen to the oxygen bond to Hem...

    For the video response portion of this assignment, your job will be to state what would happen to the oxygen bond to Hemoglobin if the pH of the tissue was the same as that of the lungs using the logic of the person’s presentation you watched. Discuss whether or not you agree with this. The video said this: Oxygen must be transported in the blood from the lungs, because the partial pressure of oxygen (pO2) is relatively high (approximately 100...

  • biochemistry if you could please help me answer the following questions! EFT i 11) (6 pts)...

    biochemistry if you could please help me answer the following questions! EFT i 11) (6 pts) Which types of symmetry are possible for a protein with six (6) identical subunits? (Select all correct answers) a) cyclic C b) cyclic C3 c) dihedral D2 d) dihedral D e) octahedral o f) icosahedral ро, Yo₂ - pO₂+ Pso 12) (6 pts) What is the fractional saturation of oxygen binding to myoglobin when the partial pressure of oxygen is 1.5 torr and dissociation...

ADVERTISEMENT
Free Homework Help App
Download From Google Play
Scan Your Homework
to Get Instant Free Answers
Need Online Homework Help?
Ask a Question
Get Answers For Free
Most questions answered within 3 hours.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT