Biochem question
1. List positive and negative effectors for oxygen binding to hemoglobin.
2.List the structural changes that occur when oxygen binds to the heme group in Mb, and in Hb
1. Hemoglobin consists of four subunits. Each heme unit contains iron in the +2 oxidation state in the centre. Each heme is capable of binding with one oxygen molecule.
The addition of oxygen is by a mechanism called allosteric addition. Basically, hemoglobin is a protein which has primary, secondary, tertiary and quaternary structures. Once oxygen binds to a heme, the oxidation state of iron changes from +2 to +3. The overall process causes a change in the quarternary structure of the heme. This makes it more conducive for the oxygen to bind to the adjacent heme in the hemoglobin molecule. So, the binding of oxygen takes place in 4 steps, not at once. Each step makes it easier for the next oxygen molecule to bind with the heme.
Negative factors are i) Oxygen concentration should be moderately good. Otherwise, the oxygen will not bind with hemoglobin. ii) Some gases like Carbon Monoxide has a much higher affinity for hemoglobin than oxygen. That is why exposure to such gases in the lack of fresh air leads to poisoning sometimes even death.
Biochem question 1. List positive and negative effectors for oxygen binding to hemoglobin. 2.List the structural...
How does BPG, or 2,3-biphophoglycerate produce the shift in the oxygen bunding curves shown? (BPG works to effect the binding of oxygen to hemoglobin) Circle the correct choice. a) BPG binds to the R state of hemoglobin tetramer. b) BPG binds to the T state of hemoglobin tetramer. c) BPG binds to the heme group, which blocks access to the oxygen d) BPG oxidizes the iron (II) in the heme group to the iron (III), preventing oxygen from binding. 1.0...
biochemistry Question 2.(12 pts) O2 binding to Fe? in one subunit of hemoglobin changes the binding affinity of the other 3 subunits. a. Describe the change in the shape of the heme that results in O2 binding. Page 4/7 b. How is the heme shape change communicated to the other subunits c. What is the role of Bisphosphoglycerate (BPG) in hemoglobin mediated oxygen transport? Question 3.(9 pts) You need to make up a 600 ml of a 40 mM solution...
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 -...
Question 24 (2 points) Which is not true about myoglobin and hemoglobin? Hemoglobin binds oxygen in the lungs and myoglobin stores oxygen in muscles Hemoglobin has 4 hemes and myoglobin has one heme Myoglobin is a simple protein made of alpha helices and hemoglobin is a conjugate protein made of alpha helices and beta sheets Hemoglobin is made of 4 myoglobin-like polypeptides
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...
List the changes that occur to the iron ion, the distal and proximal histidines, and to the α- helices that the histidines are in when oxygen binds to the iron in the heme prostethic group
Chapter 9. Hemoglobin and Myoglobin 1. Which of these is not found in myoglobin? A) alpha helix b) beta sheet c) heme group d) globular folding pattern 2. Which statement about hemoglobin is not true? A) it is globular b) it contains helix- loop-helix c) it has three subunits d) it has heme groups 3. The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these...
1. Describe how effectors of allostery regulate protein function based on positive and negative changes that take place in the protein. 2. Describe how ligand binding controls protein function by allostery 3. Describe the regulation of protein function based on quaternary structure 4. Propose how an inhibitor may or may not be an allosteric effector based on competitive, noncompetitive, and uncompetitive inhibition Describe quaternary structure based on subunits.
ter 9. Hemoglobin and Myoglobin Which of these is not found in myoglobin? A) alpha helix b) beta sheetc) heme group, d) globular folding pattern • Which statement about hemoglobin is not true? A) it is globular b) it contains helix loop-helix c) it has three subunits d) it has heme groups · The molecule which binds in the central cavity of hemoglobin when it is deoxygenated is: a) CO2 b) heme c) BPG d) all of these - The...
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...