Question

5. Based on the binding curves of different versions of myoglobin shown below: -Myoglobin type 1 -Myoglobin type 2 20 30 40 7
0 0
Add a comment Improve this question Transcribed image text
Answer #1

For a myoglobin protein and O₂ ligand equilibrio crill be P+ L € PL P= Protein La Ligand Now anociation constant kat [PL] [p]Hoca as O in ganeons in so the equation and become - pq + + At o = 0.5-5. - AA N . Þ O + + . 1 = p at a = o.s ewe which is caFor Myoglotain type - 1 At a=0.5, 102 = 20 tora. from the graph. tonn. so pso = 20 For Myoglobin type-2 I from the A A so a=0

Add a comment
Know the answer?
Add Answer to:
5. Based on the binding curves of different versions of myoglobin shown below: -Myoglobin type 1...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

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 binc ,the oxygen binding curves below for questions 3-6. The curves below represent ing to...

    oxygen binc ,the oxygen binding curves below for questions 3-6. The curves below represent ing to two types of hemoglobin-"normal" -which has a Kd of 27 torrs and a mutant form of hemoglobin called Beth Israel. The third curve shows oxygen binding to " strippe Beth Israel. 3. (2 pts) The y-asxis in Figure I represents? Clearly explain, in a few words, what this Cleary means. 4.(3pts) Clearly label the curves. HbBI for hemoglobin Beth Israel, HbA for normal hemoglobin,...

  • The following results represent the oxygen binding activity of purified myoglobin, purified hemoglobin, and hemoglobin in...

    The following results represent the oxygen binding activity of purified myoglobin, purified hemoglobin, and hemoglobin in human blood cells. pO2 (Torr) Fraction of purified myoglobin with O2 pO2 (Torr) Fraction of purified hemoglobin with O2 pO2 (Torr) Fraction of hemoglobin in red blood cells with O2 0.5 0.161 0.1 .00315 10.6 0.10 1.0 0.277 0.35 .0099 19.5 0.30 2.0 0.434 0.794 .0306 27.4 0.50 3.0 0.535 1.748 .0909 37.5 0.70 4.0 0.605 2.884 .24 50.4 0.85 6.0 0.697 4.467 .50...

  • Strong-binding YO Transition from weak- to strong-binding Weak-binding 20 40 60 80 Po, (mm Hg) 100...

    Strong-binding YO Transition from weak- to strong-binding Weak-binding 20 40 60 80 Po, (mm Hg) 100 120 Analyze the binding curve by completing the following sentences. Match the words in the left column to the appropriate blanks in the sentences on the right. View Available Hints) Reset Help decrease Of the two axes in the oxygen binding curve, the y-axis shows the increase where the percentage of bound and unbound oxygen binding sites can be determined. An axis value of...

  • biochemistry need help! 1. Answer the following series of questions related to the curve shown below for Hemoglobin...

    biochemistry need help! 1. Answer the following series of questions related to the curve shown below for Hemoglobin (Hb) and Myoglobin (Mb) binding to oxygen 1.00 p.so 0.60 0.40 0.20 0.0 C 120 80 100 60 20 40 What is the implication of the differences between the points A and C on the same binding curve? a. (ie. what does this reflect?) whertcs point 30 (condntin ofL) Pont A reaches 507 5oturaien o sleur Hd thar is a hihr Ka....

  • 1. Based on the data in the table below (a) what is the Kd for hormone...

    1. Based on the data in the table below (a) what is the Kd for hormone binding by Protein1 and Protein ? (b) Which of these proteins binds most tightly to this hormone? Work this problem on a separate piece of graph paper. Y for Protein 2 ormone concentration (nM) Yfor Protein 1 0.17 0.33 0.5 0.8 0.91 0.95 0.98 0.2 .5 5T 4 10 20 50 0.5 0.67 0.89 0.95 0.97 0.99 2. Calculate the fractional saturation of hemoglobin...

  • Based on the figure below what type of radioactive decay would you expectCu to undergo? 160...

    Based on the figure below what type of radioactive decay would you expectCu to undergo? 160 150 140 BI (n/p - 1.52) 130 120 110 100 a) alpha emission 90 (n/p = 1.40) 80 b) beta emission Number of neutrons, n 70 c) gamma emission 60 1:1 neutron- 50 to proton ratio d) 74Cu is not radioactive 40 30 20 10 Fe (n/p = 1.15) mo (n/p - 1.00) 10 20 30 40 50 60 70 80 90 100 Number...

  • 3. Answer Shown below is a binding isotherm for an enzyme called a phosphatase and a...

    3. Answer Shown below is a binding isotherm for an enzyme called a phosphatase and a lead compound known as JF99. There is a tryptophan near the binding site, and the fluorescence from this residue increases upon binding the compound (shown on the y axis). At the highest concentration of JF99 tested (1 uM), the fluorescence signal is 490 units (not shown on the graph). Estimate the value of KD- fluorescence signal (arbitrary units) ° 10 20 30 40 [JF99]...

  • 3. The following graph shows the cost and revenue curves for a firm in a perfectly...

    3. The following graph shows the cost and revenue curves for a firm in a perfectly competitive market. 90 80 D=MR 70 60 ATC Price and cost ($) 50 AVC 40 30 MC 20 10 0 10 20 30 40 50 60 70 80 90 a) Assume that new firms enter this market and that drives the price down to $35 per unit. Will the firm continue to produce or shut down? Explain your answer.

  • The graph below shows solubility curves of various ionic compounds. At 50 degrees C the solubility...

    The graph below shows solubility curves of various ionic compounds. At 50 degrees C the solubility of KNO3 is 80g per 100g of water. The solution is heated to 70 degrees C. How many more grams of potassium nitrate mistxbe added to make the solution saturated? 150 KI 140 130 120 110 NaNO3 100 KNO3 90 Grams of solute per 100 g H2O 80 70 NH3) 60 NHACI 50 -KCI Naci 40 30 20 TKCIO3 10 Cez(SO4)3 0 0 10...

  • TUUL CUNILL UNSwel. (1 mark each x 18 = 18 marks). 1. The sigmoidal shape of...

    TUUL CUNILL UNSwel. (1 mark each x 18 = 18 marks). 1. The sigmoidal shape of oxygen-binding curve of hemoglobin is due to: Tissues -- -------- Lungs Fractional Saturation Hemoglobin Myo- globin 05 - Pso=26 Oxygen 10 20 30 40 50 60 70 80 90 100 Concentration poz (torr) Figure 4.46 Principles of Biochemistry, 4/ 2006 Pearson Prentice Hall,Inc. It's unique tetrameric quaternary structure. Positive cooperative binding. axd (no 22 B Conformational changes occurs in the hemoglobin protein due to...

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
Active Questions
ADVERTISEMENT